期刊
EUROPEAN JOURNAL OF BIOCHEMISTRY
卷 270, 期 7, 页码 1528-1535出版社
BLACKWELL PUBLISHING LTD
DOI: 10.1046/j.1432-1033.2003.03519.x
关键词
sulfhydryl oxidase; mitochondrial Erv1p; redox-active CXXC; dimer formation; cysteine mutants
Yeast Erv1p is a ubiquitous FAD-dependent sulfhydryl oxidase, located in the intermembrane space of mitochondria. The dimeric enzyme is essential for survival of the cell. Besides the redox-active CXXC motif close to the FAD, Erv1p harbours two additional cysteine pairs. Site-directed mutagenesis has identified all three cysteine pairs as essential for normal function. The C-terminal cysteine pair is of structural importance as it contributes to the correct arrangement of the FAD-binding fold. Variations in dimer formation and unique colour changes of mutant proteins argue in favour of an interaction between the N-terminal cysteine pair with the redox centre of the partner monomer.
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