Cytochrome b5

Cytochrome b5
Cytochrome B5 (rat) bound to its cofactor. Haem in black, iron in red and iron-binding histidine residues shown as sticks. (PDB: 1ICC​)
Identifiers
Symbol	CYB5A
Alt. symbols	CYB5
Entrez	1528
HUGO	2570
OMIM	250790
PDB	1JEX
RefSeq	NM_001914
UniProt	P00167
Other data
Locus	Chr. 18 q23

Cytochrome b5
Identifiers
Symbol	Cyt_B5
Pfam	PF00173
InterPro	IPR001199
PROSITE	PDOC00170
Available protein structures: Pfam structures PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

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 1.1.2.3), sulfite oxidase (EC 1.8.3.1), plant and fungal nitrate reductases (EC 1.7.1.1, EC 1.7.1.2, EC 1.7.1.3), and plant and fungal cytochrome b₅/acyl lipid desaturase fusion proteins.

Structure

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 1.6.2.2 cytochrome-b₅ reductase

NADH + H⁺ + 2 ferricytochrome b₅ → NAD⁺ + 2 ferrocytochrome b₅

EC 1.10.2.1 L-ascorbate—cytochrome-b₅ reductase

L-ascorbate + ferricytochrome b₅ → monodehydroascorbate + ferrocytochrome b₅

EC 1.14.18.2 CMP-N-acetylneuraminate monooxygenase

CMP-N-acetylneuraminate + 2 ferrocytochrome b₅ + O₂ + 2 H⁺ → CMP-N-glycoloylneuraminate + 2 ferricytochrome b₅ + H₂O

EC 1.14.19.1 stearoyl-CoA 9-desaturase

stearoyl-CoA + 2 ferrocytochrome b₅ + O₂ + 2 H⁺ → oleoyl-CoA + 2 ferricytochrome b₅ + H₂O

EC 1.14.19.3 linoleoyl-CoA 9-desaturase

linoleoyl-CoA + 2 ferrocytochrome b₅ + O₂ + 2 H⁺ → γ-linolenoyl-CoA + 2 ferricytochrome b₅ + H₂O

See also

• P450-containing systems
• Cytochrome b5, type A

References

• Lederer, F. (1994). "The cytochrome b₅-fold: an adaptable module". Biochimie 76 (7): 674–692. doi:10.1016/0300-9084(94)90144-9. PMID 7893819.
• Napier, J.A., Michaelson, L.V. and Sayanova, O. (2003). "The role of cytochrome b₅ fusion desaturases in the synthesis of polyunsaturated fatty acids". Prostaglandins, Leukotrienes and Essential Fatty Acids 68 (2): 135–143. doi:10.1016/S0952-3278(02)00263-6. PMID 12538077.
• Rivera, M., Barillas-Mury, C., Christensen, K.A., Little, J.W., Wells, M.A. and Walker, F.A. (1992). "Gene synthesis, bacterial expression, and ¹H NMR spectroscopic studies of the rat outer mitochondrial membrane cytochrome b₅". Biochemistry 31 (48): 12233–12240. doi:10.1021/bi00163a037. PMID 1333795.
• Schenkman, J.B. and Jansson, I. (2003). "The many roles of cytochrome b₅". Pharmacol. Ther. 97 (2): 139–152. doi:10.1016/S0163-7258(02)00327-3. PMID 12559387.

External links

• PDB: 1B5A​ - Solution structure of rat cytochrome b₅ (form A)
• PDB: 1B5B​ - Solution structure of rat cytochrome b₅ (form B)
• PDB: 1CXY​ - X-ray structure of cytochrome b₅₅₈ from Ectothiorhodospira vacuolata
• Online 'Mendelian Inheritance in Man' (OMIM) 250790 - Methemoglobinemia due to deficiency of cytochrome b₅