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Function of cytochrome-c: Cytochrome c is a component of the electron transport chain in

mitochondria. The heme group of cytochrome c accepts electrons from the bc1 complex and
transfers electrons to the complex IV. Cytochrome c is also involved in initiation of apoptosis. Upon
release of cytochrome c to the cytoplasm, the protein binds apoptotic protease activating factor-1
(Apaf-1).[1]
Cytochrome c can catalyze several reactions such as hydroxylation and aromatic oxidation, and
shows peroxidase activity by oxidation of various electron donors such as 2,2-azino-bis(3ethylbenzthiazoline-6-sulphonic acid) (ABTS), 2-keto-4-thiomethyl butyric acid and 4aminoantipyrine.
Cytochrome: Cytochromes are, membrane-bound (i.e. inner mitochondrial membrane)
hemeproteins containing heme groups and are primarily responsible for the generation of ATP via
electron transport.
They are found either as monomeric proteins (e.g., cytochrome c) or as subunits of bigger
enzymatic complexes that catalyze redox reactions.
History: Cytochromes were initially described in 1884 by MacMunn as respiratory pigments
(myohematin or histohematin).[1] In the 1920s, Keilin rediscovered these respiratory pigments and
named them the cytochromes, or cellular pigments, and classified these heme proteins, on the
basis of the position of their lowest energy absorption band in the reduced state, as cytochromes a
(605 nm), b (~565 nm), and c (550 nm). The UV-visible spectroscopic signatures of hemes are still
used to identify heme type from the reduced bis-pyridine-ligated state, i.e., the pyridine
hemochrome method. Within each class, cytochrome a, b, or c, early cytochromes are numbered
consecutively, e.g. cyt c, cyt c1, and cyt c2, with more recent examples designated by their reduced
state R-band maximum, e.g. cyt c559.[2]
Structure and functionThe heme group is a highly conjugated ring system (which allows its
electrons to be very mobile) surrounding a metal ion, which readily interconverts between the
oxidation states. For many cytochromes, the metal ion present is that of iron, which interconverts
between Fe2+ (reduced) and Fe3+ (oxidized) states (electron-transfer processes) or between Fe2+
(reduced) and Fe3+ (formal, oxidized) states (oxidative processes). Cytochromes are, thus, capable
of performing oxidation and reduction. Because the cytochromes (as well as other complexes) are
held within membranes in an organized way, the redox reactions are carried out in the proper
sequence for maximum efficiency.
In the process of oxidative phosphorylation, which is the principal energy-generating process
undertaken by organisms, other membrane-bound and -soluble complexes and cofactors are
involved in the chain of redox reactions, with the additional net effect that protons (H+) are
transported across the mitochondrial inner membrane. The resulting transmembrane proton
gradient ([protonmotive force]) is used to generate ATP, which is the universal chemical energy
currency of life. ATP is consumed to drive cellular processes that require energy (such as synthesis
of macromolecules, active transport of molecules across the membrane, and assembly of flagella).
Types: Several kinds of cytochrome exist and can be distinguished by spectroscopy, exact
structure of the heme group, inhibitor sensitivity, and reduction potential.
Three types of cytochrome are distinguished by their prosthetic groups:Type
Cytochrome a

heme a

Cytochrome b

heme b

Cytochrome d

tetrapyrrolic chelate of iron[3]

prosthetic group

The definition of cytochrome c is not defined in terms of the heme group.[4] There is no
"cytochrome e," but there is a cytochrome f, which is often considered a type of cytochrome c.[5]
In mitochondria and chloroplasts, these cytochromes are often combined in electron transport and
related metabolic pathways:Cytochromes
Combination
a and a3
Cytochrome c oxidase ("Complex IV") with electrons delivered to complex by soluble
cytochrome c (hence the name)
b and c1

Coenzyme Q - cytochrome c reductase ("Complex III")

b6 and f

Plastoquinolplastocyanin reductase

A completely distinct family of cytochromes is known as the cytochrome P450 oxidases, so named
for the characteristic Soret peak formed by absorbance of light at wavelengths near 450 nm when
the heme iron is reduced (with sodium dithionite) and complexed to carbon monoxide. These
enzymes are primarily involved in steroidogenesis and detoxification.