The oxygen binding site of cytochrome oxidase

FEBS Letters

Welinder, Karen G.¹  Mikkelsen, Lars¹ 

[1] Institute of Biochemical Genetics, University of Copenhagen, Ø. Farimagsgade 2A, DK-1353 Copenhagen K, Denmark

关键词: Cytochrome c oxidase;    Cytochrome a 3;    Globin;    Exon;    Heme binding sequence;    Membrane buried sequence;   

DOI  :  10.1016/0014-5793(83)80553-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Analyses of heme-attached amino acid sequences in known hemoprotein superfamilies provide a basis for prediction of such sequences in hemoproteins of unknown three-dimensional structure. Among 11 histidine residues conserved in subunit I of 3 mammalian and 2 fungal cytochrome oxidases the sequence around His-233 (human) is the most conserved and shows remarkable similarity to the sequence of the oxygen binding site in globins. Furthermore, the gene coding for subunit I in Saccharomyces cerevisiae and the gene for leghemoglobin in soybean are both split by introns right after these similar histidine sequences. The predicted distal histidine sequence of subunit I provides for heme a3 and Cu_a3 binding and has an extraordinarily high content of aromatic residues. These aromatic groups may serve as a molecular electron capacitor. Transmembrane sequences and electron transfer sequences are proposed.

【 授权许可】

Unknown