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Cytochromes b5 are ubiquitous electron transport hemoproteins found in animals, plants, fungi and purple phototrophic bacteria. The microsomal and mitochondrial variants are membrane-bound, while bacterial and those from erythrocytes and other animal tissues are water-soluble. The family of cytochrome b5-like proteins includes (besides cytochrome b5 itself) hemoprotein domains covalently associated with other redox domains in flavocytochrome cytochrome b2 (L-lactate dehydrogenase; EC 220.127.116.11), sulfite oxidase (EC 18.104.22.168), plant and fungal nitrate reductases (EC 22.214.171.124, EC 126.96.36.199, EC 188.8.131.52), and plant and fungal cytochrome b5/acyl lipid desaturase fusion proteins.
Additional recommended knowledge
3-D structures of a number of cytochrome b5 and yeast flavocytochrome b2 are known. The fold belongs to the α+β class, with two hydrophobic cores on each side of a β-sheet. The larger hydrophobic core constitutes the heme-binding pocket, closed off on each side by a pair of helices connected by a turn. The smaller hydrophobic core may have only a structural role and is formed by spatially close N-terminal and C-terminal segments. The two histidine residues provide the fifth and sixth heme ligands, and the propionate edge of the heme group lies at the opening of the heme crevice. Two isomers of cytochrome b5, referred to as the A (major) and B (minor) forms, differ by a 180° rotation of the heme about an axis defined by the α- and γ-meso carbons.
Cytochrome b5 in some biochemical reactions
EC 184.108.40.206 cytochrome-b5 reductase
EC 220.127.116.11 L-ascorbate—cytochrome-b5 reductase
EC 18.104.22.168 CMP-N-acetylneuraminate monooxygenase
EC 22.214.171.124 stearoyl-CoA 9-desaturase
EC 126.96.36.199 linoleoyl-CoA 9-desaturase
|This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Cytochrome_b5". A list of authors is available in Wikipedia.|