Electron transport chain

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The electron transport chain in the mitochondrion is the site of oxidative phosphorylation in eukaryotes.

The NADH and succinate generated in the citric acid cycle are oxidized, providing energy to power ATP
synthase.

Photosynthetic electron transport chain of the thylakoid membrane.

The electron transport chain (ETC) is a series

of complexes that transfer electrons from electron donors to electron
acceptors via redox (both reduction and oxidation occurring simultaneously) reactions,
and couples this electron transfer with the transfer of protons (H+ ions) across
a membrane. The electron transport chain is built up of peptides, enzymes, and other
molecules.
The flow of electrons through the electron transport chain an exergonic process. The
energy from the redox reactions create an electrochemical proton gradient that drives
the synthesis of adenosine triphosphate (ATP). In aerobic respiration, the flow of
electrons terminates with molecular oxygen being the final electron acceptor.
In anaerobic respiration, other electron acceptors are used, such as sulfate.
In the electron transport chain, the redox reactions are driven by the Gibbs free
energy state of the components. Gibbs free energy is related to a quantity called the
redox potential. The complexes in the electron transport chain harvest the energy of the
redox reactions that occur when transferring electrons from a low redox potential to a
higher redox potential, creating an electrochemical gradient. It is the electrochemical
gradient created that drives the synthesis of ATP via coupling with oxidative
phosphorylation with ATP synthase.[1]
The electron transport chain, and site of oxidative phosphorylation is found on the inner
mitochondrial membrane. The energy stored from the process of respiration in reduced
compounds (such as NADH and FADH) is used by the electron transport chain to pump
protons into the inter membrane space, generating the electrochemical gradient over
the inner mitochrondrial membrane. In photosynthetic eukaryotes, the electron transport
chain is found on the thylakoid membrane. Here, light energy drives the reduction of
components of the electron transport chain and therefore causes subsequent synthesis
of ATP. In bacteria, the electron transport chain can vary over species but it always
constitutes a set of redox reactions that are coupled to the synthesis of ATP, through
the generation of an electrochemical gradient, and oxidative phosphorylation through
ATP synthase.[2]

Contents

 1Mitochrondrial electron transport chains

o 1.1Mitochondrial redox carriers
 1.1.1Complex I
 1.1.2Complex II
 1.1.3Complex III
 1.1.4Complex IV
o 1.2Coupling with oxidative phosphorylation
o 1.3Reverse electron flow
 2Bacterial electron transport chains
o 2.1Electron donors
o 2.2Complex I and II
o 2.3Quinone carriers
o 2.4Proton pumps
o 2.5Cytochrome electron carriers
o 2.6Terminal oxidases and reductases
o 2.7Electron acceptors
 3Photosynthetic
 4See also
 5References
 6Further reading
 7External links
Mitochrondrial electron transport chains[edit]
Most eukaryotic cells have mitochondria, which produce ATP from products of the citric
acid cycle, fatty acid oxidation, and amino acid oxidation. At the inner mitochondrial
membrane, electrons from NADH and FADH2 pass through the electron transport chain to
oxygen, which is reduced to water.[3] The electron transport chain comprises
an enzymatic series of electron donors and acceptors. Each electron donor will pass
electrons to a more electronegative acceptor, which in turn donates these electrons to
another acceptor, a process that continues down the series until electrons are passed to
oxygen, the most electronegative and terminal electron acceptor in the chain. Passage
of electrons between donor and acceptor releases energy, which is used to generate
a proton gradient across the mitochondrial membrane by "pumping" protons into the
intermembrane space, producing a thermodynamic state that has the potential to do
work. This entire process is called oxidative phosphorylation since ADP is
phosphrylated to ATP by using the electrochemical gradient established by the redox
reactions of the electron transport chain.
Mitochondrial redox carriers[edit]
Energy obtained through the transfer of electrons down the electron transport chain is
used to pump protons from the mitochondrial matrix into the intermembrane space,
creating an electrochemical proton gradient (ΔpH) across the inner mitochondrial
membrane. This proton gradient is largely but not exclusively responsible for the
mitochondrial membrane potential (ΔΨM).[4] It allows ATP synthase to use the flow of
H+ through the enzyme back into the matrix to generate ATP from adenosine
diphosphate (ADP) and inorganic phosphate. Complex I (NADH coenzyme Q
reductase; labeled I) accepts electrons from the Krebs cycle electron
carrier nicotinamide adenine dinucleotide (NADH), and passes them to coenzyme Q
(ubiquinone; labeled Q), which also receives electrons from complex II (succinate
dehydrogenase; labeled II). Q passes electrons to complex III (cytochrome bc1 complex;
labeled III), which passes them to cytochrome  c (cyt c). Cyt c passes electrons to
Complex IV (cytochrome c oxidase; labeled IV), which uses the electrons and hydrogen
ions to reduce molecular oxygen to water.
Four membrane-bound complexes have been identified in mitochondria. Each is an
extremely complex transmembrane structure that is embedded in the inner membrane.
Three of them are proton pumps. The structures are electrically connected by lipid-
soluble electron carriers and water-soluble electron carriers. The overall electron
transport chain:

NADH+H+ → Complex I → Q → Complex III → cytochrome c → Complex IV → H2O

↑
Complex II
↑
Succinate

Complex I[edit]
Further information: Respiratory complex I
In complex I (NADH ubiquinone oxireductase, Type I NADH dehydrogenase, or
mitochondrial complex I; EC 1.6.5.3), two electrons are removed from NADH and
transferred to a lipid-soluble carrier, ubiquinone (UQ). The reduced product, ubiquinol
(UQH2), freely diffuses within the membrane, and Complex I translocates four protons
(H+) across the membrane, thus producing a proton gradient. Complex I is one of the
main sites at which premature electron leakage to oxygen occurs, thus being one of the
main sites of production of superoxide.[5]
The pathway of electrons is as follows:
NADH is oxidized to NAD+, by reducing Flavin mononucleotide to FMNH2 in one two-
electron step. FMNH2 is then oxidized in two one-electron steps, through
a semiquinone intermediate. Each electron thus transfers from the FMNH 2 to an Fe-S
cluster, from the Fe-S cluster to ubiquinone (Q). Transfer of the first electron results in
the free-radical (semiquinone) form of Q, and transfer of the second electron reduces
the semiquinone form to the ubiquinol form, QH 2. During this process, four protons are
translocated from the mitochondrial matrix to the intermembrane space. [6] As the
electrons become continuously oxidized and reduced throughout the complex an
electron current is produced along the 180 Angstrom width of the complex within the
membrane. This current powers the active transport of four protons to the
intermembrane space per two electrons from NADH.[7]
Complex II[edit]
In complex II (succinate dehydrogenase or succinate-CoQ reductase; EC 1.3.5.1)
additional electrons are delivered into the quinone pool (Q) originating from succinate
and transferred (via flavin adenine dinucleotide (FAD)) to Q. Complex II consists of four
protein subunits: succinate dehydrogenase, (SDHA); succinate dehydrogenase
[ubiquinone] iron-sulfur subunit, mitochondrial, (SDHB); succinate dehydrogenase
complex subunit C, (SDHC) and succinate dehydrogenase complex, subunit D,
(SDHD). Other electron donors (e.g., fatty acids and glycerol 3-phosphate) also direct
electrons into Q (via FAD). Complex II is a parallel electron transport pathway to
complex 1, but unlike complex 1, no protons are transported to the intermembrane
space in this pathway. Therefore, the pathway through complex II contributes less
energy to the overall electron transport chain process.
Complex III[edit]
In Complex III (cytochrome bc1 complex or CoQH2-
cytochrome c reductase; EC 1.10.2.2), the Q-cycle contributes to the proton gradient by
an asymmetric absorption/release of protons. Two electrons are removed from QH 2 at
the QO site and sequentially transferred to two molecules of cytochrome  c, a water-
soluble electron carrier located within the intermembrane space. The two other
electrons sequentially pass across the protein to the Q i site where the quinone part of
ubiquinone is reduced to quinol. A proton gradient is formed by one quinol () oxidations
at the Qo site to form one quinone () at the Qi site. (In total, four protons are
translocated: two protons reduce quinone to quinol and two protons are released from
two ubiquinol molecules.)
When electron transfer is reduced (by a high membrane
potential or respiratory inhibitors such as antimycin A),
Complex III may leak electrons to molecular oxygen,
resulting in superoxide formation.
This complex is inhibited by dimercaprol (British
Antilewisite, BAL), Napthoquinone and Antimycin.
Complex IV[edit]
In Complex IV (cytochrome c oxidase; EC 1.9.3.1),
sometimes called cytochrome AA3, four electrons are
removed from four molecules of cytochrome  c and
transferred to molecular oxygen (O2), producing two
molecules of water. The complex contains coordinated
copper ions and several heme groups. At the same time,
eight protons are removed from the mitochondrial matrix
(although only four are translocated across the membrane),
contributing to the proton gradient. The exact details of
proton pumping in Complex IV are still under study. [8]
Coupling with oxidative phosphorylation[edit]

Depiction of ATP synthase, the site of oxidative phosphorylation to

generate ATP.
The chemiosmotic coupling hypothesis, proposed by Nobel
Prize in Chemistry winner Peter D. Mitchell, the electron
transport chain and oxidative phosphorylation are coupled
by a proton gradient across the inner mitochondrial
membrane. The efflux of protons from the mitochondrial
matrix creates an electrochemical gradient (proton
gradient). This gradient is used by the FOF1 ATP
synthase complex to make ATP via oxidative
phosphorylation. ATP synthase is sometimes described
as Complex V of the electron transport chain.[9] The
FO component of ATP synthase acts as an ion channel that
provides for a proton flux back into the mitochondrial
matrix. It is composed of a, b and c subunits. Protons in the
inter-membranous space of mitochondria first enters the
ATP synthase complex through a subunit channel. Then
protons move to the c subunits.[10] The number of c subunits
it has determines how many protons it will require to make
the FO turn one full revolution. For example, in humans,
there are 8 c subunits, thus 8 protons are required.
[11]
 After c subunits, protons finally enters matrix
using a subunit channel that opens into the mitochondrial
matrix.[10] This reflux releases free energy produced during
the generation of the oxidized forms of the electron carriers
(NAD+ and Q). The free energy is used to drive ATP
synthesis, catalyzed by the F1 component of the complex.[12]
Coupling with oxidative phosphorylation is a key step for
ATP production. However, in specific cases, uncoupling the
two processes may be biologically useful. The uncoupling
protein, thermogenin—present in the inner mitochondrial
membrane of brown adipose tissue—provides for an
alternative flow of protons back to the inner mitochondrial
matrix. Thyroxine is also a natural uncoupler. This
alternative flow results in thermogenesis rather than ATP
production.[13]
Reverse electron flow[edit]
Reverse electron flow, is the transfer of electrons through
the electron transport chain through the reverse redox
reactions. Usually requiring a significant amount of energy
to be used, this can result in reducing the oxidised form of
electron donors. For example, NAD+ can be reduced to
NADH by complex I.[14] There are several factors that have
been shown to induce reverse electron flow. However,
more work needs to be done to confirm this. One such
example is blockage of ATP production by ATP synthase,
resulting in a build-up of protons and therefore a
higher proton-motive force, inducing reverse electron flow.
[15]

Bacterial electron transport chains[edit]

In eukaryotes, NADH is the most important electron donor.
The associated electron transport chain is
NADH → Complex I → Q → Complex
III → cytochrome c → Complex
IV → O2 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 are several different electron
donors and several different electron acceptors. The
generalized electron transport chain in bacteria is:

Donor Donor
Donor
↓ ↓
↓
dehydrogenase → quinone →
bc1 → cytochrome
↓
↓
oxidase(reductase)
oxidase(reductase)
↓
↓
Acceptor
Acceptor

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 an electrochemical
gradient over a membrane. 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[edit]
In the present day biosphere, the most common electron
donors are organic molecules. Organisms that use organic
molecules as an electron 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 an organism is called a lithotroph ("rock-
eater"). Inorganic electron donors include hydrogen, carbon
monoxide, ammonia, nitrite, sulfur, sulfide, manganese
oxide, 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.
Complex I and II[edit]
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), electron transport chain. Some
dehydrogenases are also proton pumps; others funnel
electrons into the quinone pool. Most dehydrogenases
show induced expression in the bacterial cell in response to
metabolic needs triggered by the environment in which the
cells grow. In the case of lactate dehydrogenase in E.coli,
the enzyme is used aerobically and in combination with
other dehydrogenases. It is inducible and is expressed
when there is high concentration of DL- lactate present in
the cell.[citation needed]
Quinone carriers[edit]
Quinones are mobile, lipid-soluble carriers that shuttle
electrons (and protons) between large, relatively immobile
macromolecular complexes embedded in the membrane.
Bacteria use ubiquinone (Coenzyme Q, the same quinone
that mitochondria use) and related quinones such
as menaquinone (Vitamin K2). Archaea in the
genus Sulfolobus use caldariellaquinone.[16] The use of
different quinones is due to slightly altered redox potentials.
These changes in redox potential are caused by changes
in structure of quinone. The Change in redox potentials of
these quinones may be suited to changes in the electron
acceptors or variations of redox potentials in bacterial
complexes.[17]
Proton pumps[edit]
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).
Cytochrome electron carriers[edit]
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, electron transport chain.) 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[edit]
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 (a
facultative anaerobe) 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.
Bacterial Complex IV can be split into classes according to
the molecules act as terminal electron acceptors. Class I
oxidases are cytochrome oxidases and use oxygen as the
terminal electron acceptor. Class II oxidases are Quinol
oxidases and can use a variety of terminal electron
acceptors. Both of these classes can be subdivided into
categories based on what redox active components they
contain. E.g. Heme aa3 Class 1 terminal oxidases are
much more efficient than Class 2 terminal oxidases[1]
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[edit]
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. In aerobic bacteria
and facultative anaerobes 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.[18]
In anaerobic environments, different electron acceptors are
used, including nitrate, nitrite, ferric iron, sulfate, carbon
dioxide, and small organic molecules such as fumarate.

Photosynthetic[edit]
Further information: Light-dependent
reaction and Photosynthetic reaction center
In oxidative phosphorylation, electrons are transferred from
a low-energy electron donor such as NADH to an acceptor
such as O2) through an electron transport chain.
In photophosphorylation, the energy of sunlight is used
to create a high-energy electron donor which can
subsequently reduce redox active components. These
components are then coupled to ATP synthesis via proton
translocation by the electron transport chain. [8]
Photosynthetic electron transport chains, like the
mitochondrial chain, can be considered as a special case
of the bacterial systems. They use mobile, lipid-soluble
quinone carriers (phylloquinone and plastoquinone) and
mobile, water-soluble carriers (cytochromes, electron
transport chain.). They also contain a proton pump. The
proton pump in all photosynthetic chains resembles
mitochondrial Complex III. The commonly-held theory
of symbiogenesis believes that both organelles descended
from bacteria.

See also[edit]
 Charge-transfer complex
 CoRR hypothesis
 Electron equivalent
  Hydrogen hypothesis
 Respirasome

References[edit]
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4. ^ Zorova LD, Popkov VA, Plotnikov EY, Silachev DN,
Pevzner IB, Jankauskas SS, et al. (July
2018). "Mitochondrial membrane potential".  Analytical
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59.  doi:10.1016/j.ab.2017.07.009. PMC  5792320.  PMID 
28711444.
5. ^ Lauren, Biochemistry, Johnson/Cole, 2010, pp 598-611
6. ^ Garrett & Grisham, Biochemistry, Brooks/Cole, 2010,
pp 598-611
7. ^ Garrett R, Grisham CM (2016). biochemistry. Boston:
Cengage. p. 687.  ISBN  978-1-305-57720-6.
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9. ^ Jonckheere AI, Smeitink JA, Rodenburg RJ (March
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10. ^ Jump up to:a b Garrett RH, Grisham CM
(2012).  Biochemistry (5th ed.). Cengage learning.
p. 664.  ISBN  978-1-133-10629-6.
11. ^ Fillingame RH, Angevine CM, Dmitriev OY (November
2003). "Mechanics of coupling proton movements to c-
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13. ^ Cannon B, Nedergaard J (January 2004).  "Brown
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 14. ^ Kim BH, Gadd GM (2008). "Introduction to bacterial
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Further reading[edit]
 Fenchel T, King GM, Blackburn TH (September
2006). Bacterial Biogeochemistry: The Ecophysiology of
Mineral Cycling (2nd ed.). Elsevier. ISBN 978-0-12-103455-
9.
 Lengeler JW (January 1999). Drews G; Schlegel HG
(eds.). Biology of the Prokaryotes. Blackwell
Science. ISBN 978-0-632-05357-5.
 Nelson DL, Cox MM (April 2005).  Lehninger Principles of
Biochemistry  (4th ed.). W. H. Freeman.  ISBN  978-0-7167-
4339-2.
 Nicholls DG, Ferguson SJ (July 2002). Bioenergetics 3.
Academic Press.  ISBN  978-0-12-518121-1.
 Stumm W; Morgan JJ (1996).  Aquatic Chemistry (3rd
ed.).  John Wiley & Sons. ISBN 978-0-471-51185-4.
 Thauer RK, Jungermann K, Decker K (March 1977). "Energy
conservation in chemotrophic anaerobic
bacteria". Bacteriological Reviews. 41 (1): 100–
80.  doi:10.1128/MMBR.41.1.100-180.1977.  PMC 413997. P
MID  860983.
 White D (September 1999). The Physiology and Biochemistry
of Prokaryotes (2nd ed.).  Oxford University Press.  ISBN  978-
0-19-512579-5.
 Voet D, Voet JG (March 2004). Biochemistry. Biochemical
Education.  28  (3rd ed.).  John Wiley & Sons.
pp.  124. doi:10.1016/s0307-4412(00)00032-7. ISBN 978-0-
471-58651-7. PMID 10878303.
 Kim HS, Patel K, Muldoon-Jacobs K, Bisht KS, Aykin-Burns
N, Pennington JD, et al. (January 2010). "SIRT3 is a
mitochondria-localized tumor suppressor required for
maintenance of mitochondrial integrity and metabolism during
 stress". Cancer Cell. 17 (1): 41–
52.  doi:10.1016/j.ccr.2009.11.023. PMC  3711519.  PMID  201
29246.

External links[edit]
 Electron+Transport+Chain+Complex+Proteins at
the US National Library of Medicine Medical
Subject Headings (MeSH)
 Khan Academy, video lecture
show

Metabolism, catabolism, anabolism

show

Metabolism: Citric acid cycle enzymes

Categories: 
 Cellular respiration
 Integral membrane proteins
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 This page was last edited on 28 October 2020, at 06:34 (UTC).
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