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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]
Donor Donor
Donor
↓ ↓
↓
dehydrogenase → quinone →
bc1 → cytochrome
↓
↓
oxidase(reductase)
oxidase(reductase)
↓
↓
Acceptor
Acceptor
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]
1. ^ Jump up to: Anraku Y (June 1988). "Bacterial electron
a b
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
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