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7: Electron Transport, Oxidative Phosphorylation, and Photosynthesis - Biology

7: Electron Transport, Oxidative Phosphorylation, and Photosynthesis - Biology


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  • 7.1: Introduction
    We have seen that glycolysis generates two pyruvate molecules per glucose molecule, and that the subsequent oxidation of each pyruvate generates two Ac-S-CoA molecules. After the further oxidation of each Ac-S-CoA by the Krebs cycle, aerobic cells have captured about 30 Kcal out of the 687 Kcal potentially available from a mole of glucose in two molecules of ATP
  • 7.2: The Electron Transport Chain (ETC)
    All cells use an electron transport chain (ETC) to oxidize substrates in exergonic reactions. The electron flow from reduced substrates through an ETC is like the movement of electrons between the poles of a battery. In the case of the battery, the electron flow releases free energy to power a motor, light, cell phone, etc. In the mitochondrial ETC, electrons flow when the reduced electron (NADH, FADH2) are oxidized.
  • 7.3: Oxidative Phosphorylation
    Oxidative phosphorylation is the mechanism that by which ATP captures the free energy in the mitochondrial proton gradient. Most of the ATP made in aerobic organisms is made by oxidative phosphorylation, rather than by substrate phosphorylation (the mechanism of ATP synthesis in glycolysis or the Krebs cycle).
  • 7.4: Photosynthesis
    If respiration (reaction 1) is the complete oxidation of glucose to H2O and CO2, then photosynthesis (reaction 2) is the reduction of CO2 using electrons from H2O. Photosynthesis is thus an endergonic reaction. During photosynthesis, sunlight (specifically visible light), fuels the reduction of CO2 (summarized below)
  • 7.5: More Thoughts on the Mechanisms and Evolution of Respiration and Photosynthesis
    We can assume that the abundance of chemical energy on our cooling planet favored the formation of cells that could capture free energy from these nutrients in the absence of any oxygen. For a time, we thought that the first cells would have extracted nutrient free energy by non-oxidative, fermentation pathways. And they would have been voracious feeders, quickly depleting their environmental nutrient resources. In this scenario, the evolution of autotrophic life forms saved life from an early e
  • 7.6: Key Words and Terms

Thumbnail: The electron transport chain in the cell is the site of oxidative phosphorylation in prokaryotes. The NADH and succinate generated in the citric acid cycle are oxidized, releasing energy to power the ATP synthase. (Public Domain; Fvasconcellos).


Biochemistry : Electron Transport and Oxidative Phosphorylation

Which electron transport chain complexes would be impaired by an iron deficiency?

Complex I (NADH-CoQ reductase) contains iron-sulfur proteins, and complex II (succinate-CoQ reductase) contains both heme and iron-sulfur proteins. Thus, iron deficiency would compromise the function of complex I and II. The other enzyme complexes do not have iron-containing proteins, thus, they would not be impaired by an iron deficiency.

Example Question #1 : Electron Transport Chain Proteins And Complexes

Which electron transport chain complex would be impaired by a deficiency of copper?

Complex IV (cytochrome oxidase) contains two copper centers, and , thus a copper deficiency would result in loss of function of enzyme complex IV. The other enzyme complexes do not contain copper, thus, they would not be impaired by a copper deficiency.

Example Question #3 : Electron Transport Chain Proteins And Complexes

What would be the most immediate result if complex II of the electron transport chain suddenly stopped working?

Buildup of succinate in the mitochondrial matrix

Increase in the hydrogen ion concentration in the mitochondrial intermembrane space

Buildup of succinate in the mitochondrial matrix

Complex II of the electron transport chain catalyzes the following reaction:

It uses the enzyme succinate dehydrogenase. The immediate result of this complex's loss of function would be a buildup of succinate, since that molecule can no longer be oxidized to fumarate. The multitude of problems that can arise come from this crucial step of the citric acid cycle not being able to move forward.

Example Question #1 : Electron Transport Chain Proteins And Complexes

Which reaction of the Krebs cycle is carried out at the electron transport chain?

The conversion of succinate to fumarate is the only reaction that occurs outside of the normal Krebs cycle. Complex II of the electron transport chain has an enzyme known as succinate dehydrogenase. This enzyme is responsible for the conversion of succinate to fumarate. Fumarate is return to the cycle where it is then oxidized to malate continuing the cycle. Each of the other reactions of the Krebs cycle listed all occur in the inner mitochondrial matrix whereas the conversion of succinate to fumarate occurs at the inner mitochondrial membrane.

Example Question #5 : Electron Transport Chain Proteins And Complexes

ATP synthase works by means of __________ .

a proton gradient across the inner mitochondrial membrane

a proton gradient across the outer mitochondrial membrane

an acetyl-CoA gradient across the inner mitochondrial membrane

an acetyl-CoA gradient across the outer mitochondrial membrane

a proton gradient across the inner mitochondrial membrane

ATP synthase uses the proton gradient across the inner membrane to generate ATP. The ATP synthase is essentially like a rotary motor. The proton gradient serves as the priming of the ATP synthase. As proton are moved from the outer mitochondrial matrix back into the mitochondrial matrix they are providing mechanical energy to turn the pump. As the pump is being turned ATP synthase utilizes a unit of ADP and inorganic phosphate to generate one molecule of ATP. This is done for every three turns of the ATP synthase.

Example Question #6 : Electron Transport Chain Proteins And Complexes

Complex IV of the electron transport chain __________ .

Includes an dehydrogenase

Is responsible directly for the production of ATP from ADP and inorganic phosphate

Includes a succinate dehydrogenase

Directs electron to oxygen to form water

Directs electron to oxygen to form water

Complex IV is also known as cytochrome c oxidase because it accepts the electrons from cytochrome c and directs them towards the four electron reduction of oxygen to form two molecules of water. ATP synthase is directly responsible for the generation of ATP by utilizing one unit of ADP and one unit of inorganic phosphate along with the proton motive force (PMF). Complex II is also known as succinate dehydrogenase which is responsible for one of the reaction of the Krebs cycle: succinate to fumarate. This reaction generates one molecule of . Complex I is also known as dehydrogenase in that it oxidizes the coenzyme .

Example Question #7 : Electron Transport Chain Proteins And Complexes

Complex I of the electron transport chain __________ .

is responsible directly for the formation of water

is responsible for accepting electrons from NADH

carries electrons to oxygen

includes succinate dehydrogenase

is responsible for accepting electrons from NADH

Complex I is also called NADH-Coenzyme Q (CoQ) reductase because it transfers 2 electrons from NADH to CoQ. Complex I was formerly known as NADH dehydrogenase. This complex binds NADH and takes up two electrons.The last step of this complex is the transfer of two electrons one at a time to CoQ. The process of transferring electrons from NADH to CoQ by complex I results in the overall transport of protons from the matrix side of the inner mitochondrial membrane to the inter membrane space where the hydrogen ion concentration increases generating a proton motive force which is utilized by ATP synthase.

Example Question #8 : Electron Transport Chain Proteins And Complexes

Complex II of the electron transport chain __________ .

is responsible for accepting electrons from

includes an dehydrogenase

has a cytochrome c binding site

includes a succinate dehydrogenase

includes a succinate dehydrogenase

Complex II of the electron transport chain is generally apart of both the electron transport chain as well as the Krebs cycle. It is the the succinate dehydrogenase that carried out the conversion of succinate to fumarate in the Krebs cycle. The only enzyme of the citric acid cycle that is an integral membrane protein. The conversion of succinate to fumarate generates an . then transfers its electrons one at a time through complex II. The final step of this complex is the transfer of two electrons one at a time to coenzyme Q.

Example Question #1 : Electron Transport Chain Proteins And Complexes

In complex II of the electron transport chain which is/are the coenzyme(s) mainly oxidized?

Complex II of the electron transport chain is generally apart of both the electron transport chain as well as the Krebs cycle. It is the the succinate dehydrogenase that carried out the conversion of succinate to fumarate in the Krebs cycle. The only enzyme of the citric acid cycle that is an integral membrane protein. The conversion of succinate to fumarate generates an . then transfers its electrons one at a time through complex II. The final step of this complex is the transfer of two electrons one at a time to coenzyme Q.

Example Question #10 : Electron Transport Chain Proteins And Complexes

What is the role of ubiquinone in the electron transport chain?

Ubiquinone carries electrons from the first enzyme complex to the second enzyme complex

Ubiquinone accepts electrons directly from

Ubiquinone accepts electrons directly from

Ubiquinone carries electrons from the third enzyme complex to the fourth enzyme complex

Ubiquinone is the final step in which oxygen is reduced to water

Ubiquinone carries electrons from the first enzyme complex to the second enzyme complex

Ubiquinone functions to carry electrons in oxidative phosphorylation from the first enzyme complex to the second enzyme complex. It does not receive electrons from nor directly.

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Fermentation/Anaerobic Respiration in Plants

Incomplete oxidation of glucose in absence of oxygen is known as fermentation. The end products are carbon-dioxide and ethanol. During fermentation pyruvate is metabolized into different compounds via different processes as explained below-

  • Ethanol fermentation or alcoholic fermentation is the process of formation of ethanol and carbon-dioxide. Ethanol fermentation converts sugars such as glucose, fructose, sucrose into ethanol and carbon-dioxide. This process is used in the formation of alcoholic beverages.

Fig.4. Alcoholic Fermentation

  • Lactic acid fermentation refers to the formation of lactic acid. There are two types of lactic acid fermentation-homolactic fermentation and heterolactic fermentation. Homolactic fermentation involves the formation of lactic acid only whereas heterolactic fermentation involves formation of lactic acid as well as other acids and alcohols. Lactic acid fermentation occurs in bacterial cells as well as in muscles during physical work such as exercise.

Electron Transport Chain of Photosynthesis | Plants

The light-driven reaction of photosynthesis also called light reaction (Hill reaction), referred to as electron transport chain, were first propounded by Robert Hill in 1939. The electron transport chain of photosynthesis is initiated by absorption of light by photosystem II (P68o).

When P680 absorbs light, it is excited and its electrons are transferred to an electron acceptor molecule. Therefore, P680 becomes a strong oxidising agent, and splits a molecule of water to release oxygen. This light-dependent splitting of water molecule is called photolysis.

However, manganese, calcium and chloride ions play important roles in photolysis of water. After photolysis of water, electrons are generated, which are then passed to the oxidised P680. Now, the electron deficient P680 (as it had already transferred its electrons to an acceptor molecule) is able to restore its electrons from the water molecule.

After accepting electron from the excited P680, the primary electron acceptor is reduced. The primary electron acceptor in plants is pheophytin. The reduced acceptor which is a strong reducing agent, now donates its electrons to the downstream components of the electron transport chain.

Photosystem I (PS I):

Similar to photosystem II (P680), photosystem I (P700) is excited on absorption of light and gets oxidised, and transfers its electrons to the primary electron acceptor (pheophytin), which, in turn gets reduced. While the oxidised P700 draws electrons from photosystem II, the reduced electron acceptor of photosystem I, transfers electrons to ferredoxin and ferredoxin-NADP reductase to reduce NADP to NADPH2.

NADPH2 is a powerful reducing agent, and is utilised in the reduction of CO2 to carbohydrates in the carbon reaction of photosynthesis. The reduction of CO2 to carbohydrates requires energy in the form of ATP, produced through electron transport chain. Process of ATP formation from ADP in the presence of light in chloroplasts is called photophosphorylation.

The Light Reaction (Hill Reaction):

The light reaction is thought to be responsible for the production of a ‘reducing power’ and oxygen from water as a result of light energy. This is as follows: The light energy, after absorption by chlorophyll, splits H2O.

(i) The (H) combines with an unidentified compound (probably ferredoxin) and is passed from this to NADP.

(ii) The NADPH2 can cause the reduction of phosphoglyceric acid……. Phosphoglyceraldehyde, together with some ATP production.

(iii) The (OH) forms H2O and oxygen:

The light reaction gives rise to two very important productions:

(i) A reducing agent NADPH2 and

(ii) An energy rich compound ATP.

These two products of the light reaction are utilized in the dark phase of photosynthesis.

The energy transformations in photosynthesis are as follow:

(i) The radiant energy of an absorbed quantum is transformed into the energy of an activated pigment molecule

(pigment molecule or activated pigment)

(ii) Now the activated pigment removes an electron from the hydroxyl ion derived from the water molecule. The (OH) represents the ‘free radical’. These are uncharged, but highly reactive forms.

(iii) The free radicals react in many ways the release of oxygen and formation of free radicals of hydrogen takes place.

(iv) The H + ions from water, together with the electron attached to the pigment are transferred to certain molecules, which then carry the reducing power to other reactions.

(v)Another reaction is the recombination of the split products of water into the water molecules itself.

This reaction is strongly energy-releasing. The chloroplast puts this reaction to work by causing it to synthesize energy-rich ATP from a precursor molecule ADP and inorganic phosphate

(6) The energy of the ATP can now be used, in the reduction of CO2 to sugar by the reducing power (NADP.H) generated in the light reaction.

This way, the radiant energy has been converted to the chemical energy of the sugar molecule by passing through a photo-activated pigment, photolyzed water fragments, and ATP. The main function of light energy in photosynthesis is to produce ATP through a complex of reactions called photophosphorylation.

The subsequent reactions leading to the formation of sugar from CO2 can proceed entirely in darkness.

Photophosphorylation:

Photosynthetic phosphorylation:

With the discovery that CO2 can be assimilated in isolated chloroplasts, this came into existence that the chloroplast must contain the enzymes necessary for this assimilation and must be able to produce the ATP (adenosine tri-phosphate) essential for the formation of the main photosynthesis products.

Arnon and his co-workers (1954) demonstrated that the isolated chloroplasts can produce ATP in the presence of light. They gave the name to this process photosynthetic phosphorylation.

This was revealed for the first time that mitochondria are not the only cytoplasmic particles that produce ATP. ATP formation in chloroplasts differs from that in mitochondria in that it is free from respiratory oxidations. During this process the light energy is being converted to ATP. In other words, there is a conversion to light energy of chemical energy.

ATP is only one of the necessary requirements for the reduction of carbon dioxide to the carbohydrate level. A reductant must be formed in photosynthesis that will provide the hydrogens or electrons for this reduction. Arnon (1951) demonstrated that isolated chloroplasts are capable of reducing pyridine nucleotides in light.

The photochemical reaction and an enzyme system are capable of utilizing the reduced pyridine nucleotide as soon as this was formed, Arnon (1957) found that NADP. H2 is the reduced pyridine nucleotide in photosynthesis.

In the presence of H2O. ADP (adenosine di-phosphate) and orthophosphate (P), substrate amounts of NADP (nicotinamide adenine dinucleotide phosphate) were reduced, accompanied by the evolution of oxygen.

The equation is as follow:

As shown by the equation the evolution of one molecule of oxygen is accompanied by the reduction of two molecules of NADP and esterification of two molecules of orthophosphate. Together, ATP and NADPH2 provide the energy requirements for CO2 assimilation. Arnon gave name to this power assimilatory power (i.e., ATP + NADPH2).

According to Arnon (1967), in bacterial photosynthesis NADH2 is utilized of NADPH2.

In the late 1950’s the reduction of NADP + was thought to be associated with a soluble protein factor found in chloroplasts. Arnon et al. (1957) observed that this protein reduced NADP + accompanied by the evolution of oxygen. They termed it the ‘NADP reducing factor.’

Thereafter the NADP reducing factor was purified and called photosynthetic pyridine nucleotide reductase (PPNR), since its catalytic activity was only apparent when chloroplasts were kept in light.

Tagawa and Arnon (1962) recognized that PPNR is one of a family of nonhemenonflavin, iron-containing proteins that is universally present in chloroplasts. These proteins were given a generic name ferredoxin.

When ferredoxin was not discovered, NADP was thought to be the terminal electron acceptor of the photosynthetic light reaction. Arnon (1967) revealed that illuminated chlorophyll reacts directly with ferredoxin and not with NADP + .

The exposition of chlorophyll to light causes a flow of electrons to ferredoxin. Now the reduced ferredoxin causes the reduction of NADP + in an enzyme catalyzed reaction that is independent of light. In other words, ferredoxin is termed as terminal electron acceptor of the photosynthetic light reaction.

The reduction of NADP takes place by ferredoxin. Under normal condition, in photosynthesis ferredoxin reduced by the acceptance of an electron is immediately reoxidized by NADP + . The reduction of NADP by ferredoxin is catalyzed by ferredoxin-NADP reductase. This shows that the mechanism of NADP + reduction in photosynthesis completes in three steps.

(i) Photochemical reduction of ferredoxin

(ii) Reoxidation of ferredoxin by ferredoxin NADP + reductase and

(iii) Reoxidation of ferredoxin-NADP + reductase by NADP + .

According to Arnon there are two types of photophosphorylation:

(i) Non-cyclic photophosphorylation and

(ii) Cyclic photophosphorylation.

Non-Cyclic Photophosphorylation:

This is a result of an interaction of photosystem I (PSI) and photosystem II (PSII). In non-cyclic photophosphorylation, the electron is not returned to the chlorophyll molecule, but is taken up by NADP ± which thereafter reduces to NADPH. Here the electron that returns to the chlorophyll molecule is derived from an outside source which is water.

In this process oxygen is released and both NADPH2 − and ATP are formed. In green plants and many photosynthetic bacteria, however, illumination is known to produce also NADPH2 − which provides hydrogen for the reduction of carbon dioxide in the day.

The electron lost by the excited chlorophyll is accepted by NADP along with a proton resulting in the formation of NADPH2. The light energy is now stored in the NADPH2 molecule. The proton required for the reduction of NADP is released from the dissociation of water molecule by photolysis into hydrogen H ± and hydroxyl ions OH.

The hydroxyl ions react to produce water and molecular oxygen.

The reaction is as follows:

Here the hydroxyl ion also releases an electron that is accepted by the cytochromes of the chloroplast. In turn, the cytochrome donates this electron to the chlorophyll molecule, which already lost an electron earlier. The energy released during this transfer of electron from the cytochrome is utilized in the formation of ATP by the photophosphorylation of ADP.

In water molecule hydrogen is strongly bound to oxygen and this can be cleaved only by the use of energy. This energy is supplied by light. This way, in non-cyclic photophosphorylation light energy takes part in two processes, i.e., the activation of chlorophyll molecule and photolysis (cleavage) of water.

In non-cyclic photophosphorylation one molecule of NADPH2 and one molecule of ATP are produced by the activation of chlorophyll molecule by a photon, while in cyclic photophosphorylation two molecules of ATP are produced for each photon absorbed by chlorophyll.

The overall reaction of photophosphorylation is as follows:

Cyclic Photophosphorylation:

When non-cyclic photophosphorylation is stopped under certain conditions, cyclic photophosphorylation takes place. The non-cyclic photophosphorylation can be stopped by illuminating isolated chloroplasts with light of wavelength greater than 680 nm.

By this way, only photosystem I (PS I) is activated, as it has a maximum absorption at 700 nm, and photosystem II (PS II), which absorbs at 680 nm, remains inactivated.

Due to inactivation of PS II, the electron flow from water to NADP is stopped, and also CO2 fixation is retarded.

When CO2 fixation stops, electrons are not removed from reduced NADPH. Thus, NADPH will not be oxidised and NADP will not be available as an electron acceptor.

Under above-mentioned conditions, cyclic-photophosphorylation occurs.

During cyclic-photophosphorylation, electrons from photosystem I (PS I) are not passed to NADP from the electron acceptor, as NADP is not available in oxidised state to receive electrons.

Hence, the electrons are transferred back to P700.

This type of movement of electrons from an electron acceptor to P700 result in the formation of ATP from ADP, and the process is called cyclic photophosphorylation.

During cyclic photophosphorylation oxygen is not released, as there is no photolysis of water and NADPH2 is also not produced.

In cyclic photophosphorylation the excited electron lost by the chlorophyll is returned to it through vitamin K or FMN (flavin mononucleotide) and cytochromes. The chlorophyll molecule on losing an electron assumes a positive charge and subsequently the electron is transferred to a second acceptor.

This second acceptor is a group of substances collectively known as cytochrome system. All the members of cytochrome system are variants of cytochrome. Ultimately these cytochromes transfer the electron to the chlorophyll molecule from where it was lost initially.

The electromagnetic energy of the light is utilized in the formation of ATP. This means that light energy is being converted into chemical energy. Here the electron after leaving a chlorophyll travels in a cyclic way and ultimately returns to the same molecule from which it initiated, and therefore, this process has been termed by Arnon as cyclic photophosphorylation.

The final electron acceptor and the initial electron donor is the same substance—the chlorophyll. No outside material takes part in the process. During cyclic photophosphorylation, one electron and two ATP molecules are formed.

One ATP molecule is being formed when the electron travels from the cofactor (i.e., vitamin K or FMN) to the cytochromes while the other when it travels from the cytochromes back to the chlorophyll molecule.

Here the light energy is being converted into chemical energy.

In nature both processes of photophosphorylation proceed simultaneously. In green plants the non-cyclic electron transfer is essential for the production of NADPH2 and ATP.

The oxygen is evolved during the process. The cyclic electron transfer fulfils the requirement of the low yield of ATP during non-cyclic process. This way, the complete light phase of photophosphorylation produces ATP and NADPH2 and oxygen is evolved.

NADPH2 is a biological reductant that brings about the reduction of carbon dioxide to carbohydrates in the dark phase of photosynthesis. Here both NADPH2 and ATP provide energy for reduction. The assimilatory power of the cell is constituted by these two components. The energy of these components is derived from visible part of sunlight.

In the dark phase of photosynthesis the energy that is stored in NADPH2 and ATP, is being transferred to the molecules of organic substances and stored there in the form of chemical energy.

During photosynthesis the electromagnetic energy of visible light is being converted into chemical energy. Now this energy is utilized by living cells as the driving force for various vital activities. This act of the conversion of energy is brought about by the photosynthetic cells of green plants or photosynthetic bacteria.

Here the solar energy is trapped by the chlorophyll apparatus. As soon as the light energy is being transformed into chemical energy, it may be used in the formation of carbohydrates, protein synthesis and other important vital activities.

The living are so designed that they can use only chemical energy for various metabolic activities. The light energy cannot be directly used for these vital activities. The light reaction of the higher plants takes place in the grana of the chloroplasts.


Roughly, around 30-32 ATP is produced from one molecule of glucose in cellular respiration. However, the number of ATP molecules generated from the breakdown of glucose varies between species. The number of H + ions that the electron transport chain pumps differ within them.

From a single molecule of glucose producing two ATP molecules in glycolysis and another two in the citric acid cycle, all other ATPs are produced through oxidative phosphorylation. Based on the experiment, it is obtained that four H + ions flow back through ATP synthase to produce a single molecule of ATP. After moving through the electron transport chain, each NADH yields 2.5 ATP, whereas each FADH2 yields 1.5 ATP.

Given below is a table showing the breakdown of ATP formation from one molecule of glucose through the electron transport chain:

Name of the PathwayNet Yield of ATP
Glycolysis2 ATP (direct) + 3-5 ATP (from 2 NADH)
Oxidation of Pyruvate5 ATP (from 2 NADH)
Citric Acid Cycle2 ATP (from 2 GTP), 15 ATP (from 6 NADH) + 3 ATP (from 2 FADH2)
Total32 ATP

As given in the table, the ATP yield from NADH made in glycolysis is not precise. The reason is that glycolysis occurs in the cytosol, which needs to cross the mitochondrial membrane to participate in the electron transport chain. Cells with a shuttle system to transfer electrons to the transport chain via FADH2 are found to produce 3 ATP from 2 NADH. In others, the delivery of electrons is done through NADH, where they produce 5 ATP molecules.


8.1.6 Explain the relationship between the structure of the mitochondrion and its function.

Matrix: Watery substance that contains ribosomes and many enzymes. These enzymes are vital for the link reaction and the Krebs cycle.

Inner membrane: The electron transport chain and ATP synthase are found in this membrane. These are vital for oxidative phosphorylation.

Space between inner and outer membranes: Small volume space into which protons are pumped into. Due to its small volume, a high concentration gradient can be reached very quickly. This is vital for chemiosmosis.

Outer membrane: This membrane separates the contents of the mitochondrion from the rest of the cell. It creates a good environment for cell respiration.

Cristae: These tubular projections of the inner membrane increase the surface area for oxidative phosphorylation.


Electron transport chains in bacteria

In eukaryotes, NADH is the most important electron donor. The associated electron transport chain is

NADHComplex IQComplex IIIcytochrome cComplex IVO2 where Complexes I, III and IV are proton pumps, while Q and cytochrome c are mobile electron carriers. The electron acceptor is molecular oxygen.

In prokaryotes (bacteria and archaea) the situation is more complicated, because there is a number of different electron donors and a number of different electron acceptors. The generalized electron transport chain in bacteria is:

Note that electrons can enter the chain at three levels: at the level of a dehydrogenase, at the level of the quinone pool, or at the level of a mobile cytochrome electron carrier. These levels correspond to successively more positive redox potentials, or to successively decreased potential differences relative to the terminal electron acceptor. In other words, they correspond to successively smaller Gibbs free energy changes for the overall redox reaction Donor → Acceptor.

Individual bacteria use multiple electron transport chains, often simultaneously. Bacteria can use a number of different electron donors, a number of different dehydrogenases, a number of different oxidases and reductases, and a number of different electron acceptors. For example, E. coli (when growing aerobically using glucose as an energy source) uses two different NADH dehydrogenases and two different quinol oxidases, for a total of four different electron transport chains operating simultaneously.

A common feature of all electron transport chains is the presence of a proton pump to create a transmembrane proton gradient. Bacterial electron transport chains may contain as many as three proton pumps, like mitochondria, or they may contain only one or two. They always contain at least one proton pump.

Electron donors

In the present day biosphere, the most common electron donors are organic molecules. Organisms that use organic molecules as an energy source are called organotrophs. Organotrophs (animals, fungi, protists) and phototrophs (plants and algae) constitute the vast majority of all familiar life forms.

Some prokaryotes can use inorganic matter as an energy source. Such organisms are called lithotrophs ("rock-eaters"). Inorganic electron donors include hydrogen, carbon monoxide, ammonia, nitrite, sulfur, sulfide, and ferrous iron. Lithotrophs have been found growing in rock formations thousands of meters below the surface of Earth. Because of their volume of distribution, lithotrophs may actually outnumber organotrophs and phototrophs in our biosphere.

The use of inorganic electron donors as an energy source is of particular interest in the study of evolution. This type of metabolism must logically have preceded the use of organic molecules as an energy source.

Dehydrogenases

Bacteria can use a number of different electron donors. When organic matter is the energy source, the donor may be NADH or succinate, in which case electrons enter the electron transport chain via NADH dehydrogenase (similar to Complex I in mitochondria) or succinate dehydrogenase (similar to Complex II). Other dehydrogenases may be used to process different energy sources: formate dehydrogenase, lactate dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase, H2 dehydrogenase (hydrogenase), etc. Some dehydrogenases are also proton pumps others simply funnel electrons into the quinone pool.

Most dehydrogenases are synthesized only when needed. Depending on the environment in which they find themselves, bacteria select different enzymes from their DNA library and synthesize only those that are needed for growth. Enzymes that are synthesized only when needed are said to be inducible.

Quinone carriers

Quinones are mobile, lipid-soluble carriers that shuttles electrons (and protons) between large, relatively immobile macromolecular complexes imbedded in the membrane. Bacteria use ubiquinone (the same quinone that mitochondria use) and related quinones such as menaquinone.

Proton pumps

A proton pump is any process that creates a proton gradient across a membrane. Protons can be physically moved across a membrane this is seen in mitochondrial Complexes I and IV. The same effect can be produced by moving electrons in the opposite direction. The result is the disappearance of a proton from the cytoplasm and the appearance of a proton in the periplasm. Mitochondrial Complex III uses this second type of proton pump, which is mediated by a quinone (the Q cycle).

Some dehydrogenases are proton pumps others are not. Most oxidases and reductases are proton pumps, but some are not. Cytochrome bc1 is a proton pump found in many, but not all, bacteria (it is not found in E. coli). As the name implies, bacterial bc1 is similar to mitochondrial bc1 (Complex III).

Proton pumps are the heart of the electron transport process. They produce the transmembrane electrochemical gradient that supplies energy to the cell.

Cytochrome electron carriers

Cytochromes are pigments that contain iron. They are found in two very different environments.

Some cytochromes are water-soluble carriers that shuttle electrons to and from large, immobile macromolecular structures imbedded in the membrane. The mobile cytochrome electron carrier in mitochondria is cytochrome c. Bacteria use a number of different mobile cytochrome electron carriers.

Other cytochromes are found within macromolecules such as Complex III and Complex IV. They also function as electron carriers, but in a very different, intramolecular, solid-state environment.

Electrons may enter an electron transport chain at the level of a mobile cytochrome or quinone carrier. For example, electrons from inorganic electron donors (nitrite, ferrous iron, etc.) enter the electron transport chain at the cytochrome level. When electrons enter at a redox level greater than NADH, the electron transport chain must operate in reverse to produce this necessary, higher-energy molecule.

Terminal oxidases and reductases

When bacteria grow in aerobic environments, the terminal electron acceptor (O2) is reduced to water by an enzyme called an oxidase. When bacteria grow in anaerobic environments, the terminal electron acceptor is reduced by an enzyme called a reductase.

In mitochondria the terminal membrane complex (Complex IV) is cytochrome oxidase. Aerobic bacteria use a number of different terminal oxidases. For example, E. coli does not have a cytochrome oxidase or a bc1 complex. Under aerobic conditions, it uses two different terminal quinol oxidases (both proton pumps) to reduce oxygen to water.

Anaerobic bacteria, which do not use oxygen as a terminal electron acceptor, have terminal reductases individualized to their terminal acceptor. For example, E. coli can use fumarate reductase, nitrate reductase, nitrite reductase, DMSO reductase, or trimethylamine-N-oxide reductase, depending on the availability of these acceptors in the environment.

Most terminal oxidases and reductases are inducible. They are synthesized by the organism as needed, in response to specific environmental conditions.

Electron acceptors

Just as there are a number of different electron donors (organic matter in organotrophs, inorganic matter in lithotrophs), there are a number of different electron acceptors, both organic and inorganic. If oxygen is available, it is invariably used as the terminal electron acceptor, because it generates the greatest Gibbs free energy change and produces the most energy.

In anaerobic environments, different electron acceptors are used, including nitrate, nitrite, ferric iron, sulfate, carbon dioxide, and small organic molecules such as fumarate.

Since electron transport chains are redox processes, they can be described as the sum of two redox pairs. For example, the mitochondrial electron transport chain can be described as the sum of the NAD + /NADH redox pair and the O2/H2O redox pair. NADH is the electron donor and O2 is the electron acceptor.

Not every donor-acceptor combination is thermodynamically possible. The redox potential of the acceptor must be more positive than the redox potential of the donor. Furthermore, actual environmental conditions may be far different from standard conditions (1 molar concentrations, 1 atm partial pressures, pH = 7), which apply to standard redox potentials. For example, hydrogen-evolving bacteria grow at an ambient partial pressure of hydrogen gas of 10 -4 atm. The associated redox reaction, which is thermodynamically favorable in nature, is thermodynamically impossible under “standard” conditions.

Summary

Bacterial electron transport pathways are, in general, inducible. Depending on their environment, bacteria can synthesize different transmembrane complexes and produce different electron transport chains in their cell membranes. Bacteria select their electron transport chains from a DNA library containing multiple possible dehydrogenases, terminal oxidases and terminal reductases. The situation is often summarized by saying that electron transport chains in bacteria are branched, modular, and inducible.


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277 Results

Reviews selected issues including learning, cognition, perception, foraging and feeding, migration and .

Reviews selected issues including learning, cognition, perception, foraging and feeding, migration and navigation, defense, and social activities including conflict, collaboration, courtship and reproduction, and communication. The interacting contributions of environment and heredity are examined and the approaches of psychology, ethology, and ecology to this area of study are treated. The relation of human behavior patterns to those of nonhuman animals is explored. Additional readings and a paper are required for graduate credit.

This course studies the relations of affect to cognition and behavior, feeling .

This course studies the relations of affect to cognition and behavior, feeling to thinking and acting, and values to beliefs and practices. These connections will be considered at the psychological level of organization and in terms of their neurobiological and sociocultural counterparts.

This class analyzes complex biological processes from the molecular, cellular, extracellular, and .

This class analyzes complex biological processes from the molecular, cellular, extracellular, and organ levels of hierarchy. Emphasis is placed on the basic biochemical and biophysical principles that govern these processes. Examples of processes to be studied include chemotaxis, the fixation of nitrogen into organic biological molecules, growth factor and hormone mediated signaling cascades, and signaling cascades leading to cell death in response to DNA damage. In each case, the availability of a resource, or the presence of a stimulus, results in some biochemical pathways being turned on while others are turned off. The course examines the dynamic aspects of these processes and details how biochemical mechanistic themes impinge on molecular/cellular/tissue/organ-level functions. Chemical and quantitative views of the interplay of multiple pathways as biological networks are emphasized. Student work will culminate in the preparation of a unique grant application in an area of biological networks.

Short, animated videos on many Anatomy and Physiology topics. Videos used in .

Short, animated videos on many Anatomy and Physiology topics. Videos used in college courses and cover the content presented in the first 2 semesters of Anatomy and Physiology for Nursing/Allied Health students.

Most of the major categories of adaptive behavior can be seen in .

Most of the major categories of adaptive behavior can be seen in all animals. This course begins with the evolution of behavior, the driver of nervous system evolution, reviewed using concepts developed in ethology, sociobiology, other comparative studies, and in studies of brain evolution. The roles of various types of plasticity are considered, as well as foraging and feeding, defensive and aggressive behavior, courtship and reproduction, migration and navigation, social activities and communication, with contributions of inherited patterns and cognitive abilities. Both field and laboratory based studies are reviewed and finally, human behavior is considered within the context of primate studies.

The lessons presented in this module on animal diversity are based on .

The lessons presented in this module on animal diversity are based on the social constructivist theory of learning. Learners construct their own understanding and develop their own skills, both individually and as part of a peer group. The activities presented here will help you, but a large part of the responsibility rests on you, in the aim of fostering learner empowerment.

The extreme challenges of life in the polar regions require the animals .

The extreme challenges of life in the polar regions require the animals who make their habitat there to make many adaptations. This unit explores the polar climate and how animals like reindeer, polar bears, penguins, sea life and even humans manage to survive there. It looks at the adaptations to physiological proceses, the environmental effects on diet, activity and fecundity, and contrasts the strategies of aquatic and land-based animals in surviving in this extreme habitat. This unit builds on and develops ideas from two other 'Animals at the extreme' units: The desert environment (S324_1) and Hibernation and torpor (S324_2).

The lethal poison Ricin (best known as a weapon of bioterrorism), Diphtheria .

The lethal poison Ricin (best known as a weapon of bioterrorism), Diphtheria toxin (the causative agent of a highly contagious bacterial disease), and the widely used antibiotic tetracycline have one thing in common: They specifically target the cell's translational apparatus and disrupt protein synthesis. In this course, we will explore the mechanisms of action of toxins and antibiotics, their roles in everyday medicine, and the emergence and spread of drug resistance. We will also discuss the identification of new drug targets and how we can manipulate the protein synthesis machinery to provide powerful tools for protein engineering and potential new treatments for patients with devastating diseases, such as cystic fibrosis and muscular dystrophy. This course is one of many Advanced Undergraduate Seminars offered by the Biology Department at MIT. These seminars are tailored for students with an interest in using primary research literature to discuss and learn about current biological research in a highly interactive setting. Many instructors of the Advanced Undergraduate Seminars are postdoctoral scientists with a strong interest in teaching.

How a cell infected by a virus signals cytotoxic T lymphocytes to .

How a cell infected by a virus signals cytotoxic T lymphocytes to kill the cell before the virus replicates and spreads. This video is two minutes and 34 seconds in length, and available in Quick Time (11 MB) and Windows Media Player (23 MB). All Infection Disease Animations are located at: http://www.hhmi.org/biointeractive/disease/animations.html.

In this class we will learn about how the process of DNA .

In this class we will learn about how the process of DNA replication is regulated throughout the cell cycle and what happens when DNA replication goes awry. How does the cell know when and where to begin replicating its DNA? How does a cell prevent its DNA from being replicated more than once? How does damaged DNA cause the cell to arrest DNA replication until that damage has been repaired? And how is the duplication of the genome coordinated with other essential processes? We will examine both classical and current papers from the scientific literature to provide answers to these questions and to gain insights into how biologists have approached such problems. This course is one of many Advanced Undergraduate Seminars offered by the Biology Department at MIT. These seminars are tailored for students with an interest in using primary research literature to discuss and learn about current biological research in a highly interactive setting. Many instructors of the Advanced Undergraduate Seminars are postdoctoral scientists with a strong interest in teaching.

Introduction to Microscopy Lab Measurement Lab History of Life Lab Phylogeny Lab .

Introduction to Microscopy Lab
Measurement Lab
History of Life Lab
Phylogeny Lab
Prokaryotes Lab I
Prokaryotes Lab II
Supergroups Excavata and Amoebozoa
Supergroup SAR
Supergroup Archaeplastida I – red algae, green algae, charophytes, seedless plants
Supergroup Archaeplastida II – seed plants
Supergroup Opisthokonta – Fungi
Supergroup Opisthokonta – Basal Animals and Deuterostomes
Supergroup Opisthokonta – Protostomes

Table of Contents Chapter 1: Cell Tour, Life’s Properties and Evolution, Studying .

Table of Contents
Chapter 1: Cell Tour, Life’s Properties and Evolution, Studying Cells
Chapter 2: Basic Chemistry, Organic Chemistry and Biochemistry
Chapter 3: Details of Protein Structure
Chapter 4: Bioenergetics
Chapter 5: Enzyme Catalysis and Kinetics
Chapter 6: Glycolysis, the Krebs Cycle and the Atkins Diet
Chapter 7: Electron Transport, Oxidative Phosphorylation and Photosynthesis
Chapter 8: DNA Structure, Chromosomes and Chromatin
Chapter 9: Details of DNA Replication & DNA Repair
Chapter 10: Transcription and RNA Processing
Chapter 11: The Genetic Code and Translation
Chapter 12: Regulation of Transcription and Epigenetic Inheritance
Chapter 13: Post-Transcriptional Regulation of Gene Expression
Chapter 14: Repetitive DNA, A Eukaryotic Genomic Phenomenon
Chapter 15: DNA Technologies
Chapter 16: Membrane Structure
Chapter 17: Membrane Function
Chapter 18: The Cytoskeleton and Cell Motility
Chapter 19: Cell Division and the Cell Cycle
Chapter 20: The Origins of Life

" Where do new drugs and treatments come from? This class will .

" Where do new drugs and treatments come from? This class will take you from the test tubes and mice of the laboratory to the treatment of patients with deadly blood disorders. Students will learn how to think as a scientist through discussion of primary research papers describing the discoveries of several novel treatments. Topics such as gene therapy, the potential of drugs based on RNA interference and the reprogramming of somatic cells into stem cells for regenerative medicine will be discussed. This course is one of many Advanced Undergraduate Seminars offered by the Biology Department at MIT. These seminars are tailored for students with an interest in using primary research literature to discuss and learn about current biological research in a highly interactive setting. Many instructors of the Advanced Undergraduate Seminars are postdoctoral scientists with a strong interest in teaching."

Antibodies, antigens, antigen-antibody reactions, cells and tissues of lymphoreticular and hematopoietic systems, .

Antibodies, antigens, antigen-antibody reactions, cells and tissues of lymphoreticular and hematopoietic systems, and individual and collective components of cell-mediated and humoral immune response.

This course focuses on the interaction of chemical engineering, biochemistry, and microbiology. .

This course focuses on the interaction of chemical engineering, biochemistry, and microbiology. Mathematical representations of microbial systems are featured among lecture topics. Kinetics of growth, death, and metabolism are also covered. Continuous fermentation, agitation, mass transfer, and scale-up in fermentation systems, and enzyme technology round out the subject material.

Our goal is to present the key observations and unifying concepts upon .

Our goal is to present the key observations and unifying concepts upon which modern biology is based it is not a survey of all biology! Once understood, these foundational observations and concepts should enable you to approach any biological process, from disease to kindness, from a scientific perspective. To understand biological systems we need to consider them from two complementary perspectives how they came to be (the historic, that is, evolutionary) and how their structures, traits, and behaviors are produced (the mechanistic, that is, the physicochemical).

Table of Contents
Chapter 1: Understanding science & thinking scientifically
Chapter 2: Life's diversity and origins
Chapter 3: Evolutionary mechanisms and the diversity of life
Chapter 4: Social evolution and sexual selection
Chapter 5: Molecular interactions, thermodynamics & reaction coupling
Chapter 6: Membrane boundaries and capturing energy
Chapter 7: The molecular nature of heredity
Chapter 8: Peptide bonds, polypeptides and proteins
Chapter 9: Genomes, genes, and regulatory networks
Chapter 10: Social systems

This exercise contains two interrelated modules that introduce students to modern biological .

This exercise contains two interrelated modules that introduce students to modern biological techniques in the area of Bioinformatics, which is the application of computer technology to the management of biological information. The need for Bioinformatics has arisen from the recent explosion of publicly available genomic information, such as that resulting from the Human Genome Project.

Covers the basics of R software and the key capabilities of the .

Covers the basics of R software and the key capabilities of the Bioconductor project (a widely used open source and open development software project for the analysis and comprehension of data arising from high-throughput experimentation in genomics and molecular biology and rooted in the open source statistical computing environment R), including importation and preprocessing of high-throughput data from microarrays and other platforms. Also introduces statistical concepts and tools necessary to interpret and critically evaluate the bioinformatics and computational biology literature. Includes an overview of of preprocessing and normalization, statistical inference, multiple comparison corrections, Bayesian Inference in the context of multiple comparisons, clustering, and classification/machine learning.

More advanced treatment of biochemical mechanisms that underlie biological processes. Emphasis on .

More advanced treatment of biochemical mechanisms that underlie biological processes. Emphasis on experimental methods used to unravel these processes, and how these processes fit into the cellular context and coordinate regulation of these processes. Topics include macromolecular machines for energy and force transduction, regulation of biosynthetic and degradative pathways, and structure and function of nucleic acids.

Imagine you are a salesman needing to visit 100 cities connected by .

Imagine you are a salesman needing to visit 100 cities connected by a set of roads. Can you do it while stopping in each city only once? Even a supercomputer working at 1 trillion operations per second would take longer than the age of the universe to find a solution when considering each possibility in turn. In 1994, Leonard Adleman published a paper in which he described a solution, using the tools of molecular biology, for a smaller 7-city example of this problem. His paper generated enormous scientific and public interest, and kick-started the field of Biological Computing, the main subject of this discussion based seminar course. Students will analyze the Adleman paper, and the papers that preceded and followed it, with an eye for identifying the engineering and scientific aspects of each paper, emphasizing the interplay of these two approaches in the field of Biological Computing. This course is appropriate for both biology and non-biology majors. Care will be taken to fill in any knowledge gaps for both scientists and engineers.


Watch the video: Oxidative phosphorylation and the electron transport chain. Khan Academy (December 2022).