Functional sulfurtransferase is associated with mitochondrial complex I from Yarrowia lipolytica, but is not required for assembly of its iron-sulfur clusters |
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Authors: | Abdrakhmanova Albina Dobrynin Krzysztof Zwicker Klaus Kerscher Stefan Brandt Ulrich |
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Institution: | Ulrich Brandt, Universit?t Frankfurt, Fachbereich Medizin, Zentrum der Biologischen Chemie, Molekulare Bioenergetik, Theodor-Stern-Kai 7, Haus 26, 60590 Frankfurt am Main, Germany. |
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Abstract: | 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. |
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Keywords: | BN-PAGE blue-native polyacrylamide gel electrophoresis DBQ n-decylubiquinone dNADH deamino-nicotinamide-adenine-dinucleotide (reduced form) dSDS-PAGE doubled sodium dodecylsulfate-polyacrylamide gel electrophoresis HAR hexa-ammine-ruthenium(III)-chloride MALDI-TOF MS matrix-assisted laser desorption/ionisation-time of flight mass spectrometry MST 3-mercaptopyruvate sulfurtransferase TST thiosulfate sulfurtransferase |
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