Cytochrome

redox active proteins containing a heme with a Fe atom as a cofactor From Wikipedia, the free encyclopedia

Cytochrome

Cytochromes are haemoproteins (or proteins containing haem groups). They make ATP by electron transport.

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Cytochrome c with heme c.

They are found either as single (monomeric) proteins (e.g., cytochrome c) or as part of bigger enzyme complexes which catalyze redox reactions.

The haem group does the redox reactions. These include all chemical reactions in which atoms have their oxidation state changed. In general, redox reactions involve the transfer of electrons.

History

Cytochromes were described in 1884 as respiratory pigments. They include (haemoglobin, myoglobin, haemocyanin, haemoerythrin and chlorocruorin.[1][2] In the 1920s, Keilin rediscovered these respiratory pigments. He called them the cytochromes, or “cellular pigments”, and classified them as haem proteins.

Types

Several kinds of cytochrome exist and can be distinguished by spectroscopy. Three types of cytochrome are distinguished by their prosthetic groups.[3] In mitochondria and chloroplasts, these cytochromes are often combined in electron transport and related metabolic pathways.

References

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