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Functional sulfurtransferase is associated with mitochondrial complex I from Yarrowia lipolytica , but is not required for assembly of its iron–sulfur clusters
Author(s) -
Abdrakhmanova Albina,
Dobrynin Krzysztof,
Zwicker Klaus,
Kerscher Stefan,
Brandt Ulrich
Publication year - 2005
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/j.febslet.2005.11.008
Subject(s) - yarrowia , rhodanese , sulfurtransferase , biochemistry , thiosulfate , sulfur , respiratory chain , sulfur metabolism , iron–sulfur cluster , chemistry , cyanide , biology , yeast , mitochondrion , enzyme , organic chemistry , cysteine
Here, we report that in the obligate aerobic yeast Yarrowia lipolytica , a protein exhibiting rhodanese (thiosulfate:cyanide sulfurtransferase) activity is associated with proton pumping NADH:ubiquinone oxidoreductase (complex I). Complex I is a key enzyme of the mitochondrial respiratory chain that contains eight iron–sulfur clusters. From a rhodanese deletion strain, we purified functional complex I that lacked the additional protein but was fully assembled and displayed no functional defects or changes in EPR signature. In contrast to previous suggestions, this indicated that the sulfurtransferase associated with Y. lipolytica complex I is not required for assembly of its iron–sulfur clusters.