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Involvement of mitochondrial ferredoxin and Cox15p in hydroxylation of heme O
Author(s) -
Barros Mario H.,
Carlson Christopher G.,
Glerum D.Moira,
Tzagoloff Alexander
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02249-9
Subject(s) - adrenodoxin , ferredoxin , heme , mutant , biochemistry , heme a , hydroxylation , chemistry , saccharomyces cerevisiae , schizosaccharomyces pombe , cytochrome p450 reductase , cytochrome c oxidase , schizosaccharomyces , mitochondrion , yeast , biology , cytochrome , coenzyme q – cytochrome c reductase , gene , enzyme , cytochrome c
Cox15p is essential for the biogenesis of cytochrome oxidase [Glerum et al., J. Biol. Chem. 272 (1997) 19088–19094]. We show here that cox15 mutants are blocked in heme A but not heme O biosynthesis. In Schizosaccharomyces pombe COX15 is fused to YAH1 , the yeast gene for mitochondrial ferredoxin (adrenodoxin). A fusion of Cox15p and Yah1p in Saccharomyces cerevisiae rescued both cox15 and yah1 null mutants. This suggests that Yah1p functions in concert with Cox15p. We propose that Cox15p functions together with Yah1p and its putative reductase (Arh1p) in the hydroxylation of heme O.