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Studies on the proton-translocating NADH:ubiquinone oxidoreductases of mitochondria and Escherichia coli using the inhibitor 1,10-phenanthroline.

作者信息

Finel M, Majander A

机构信息

Helsinki Bioenergetics Group, Department of Medical Chemistry, University of Helsinki, Finland.

出版信息

FEBS Lett. 1994 Feb 14;339(1-2):142-6. doi: 10.1016/0014-5793(94)80402-8.

DOI:10.1016/0014-5793(94)80402-8
PMID:8313963
Abstract

Mitochondrial NADH:ubiquinone oxidoreductase (complex I) is uncompetitively inhibited by 1,10-phenanthroline (OP). EPR spectroscopy of submitochondrial particles indicates that OP, similarly to rotenone, inhibits electron transfer between the Fe-S clusters of complex I and the ubiquinone pool. The proton-translocating NADH dehydrogenase (NDH1) of E. coli is more sensitive to OP than is NDH1 of Paracoccus. EPR spectroscopy of membranous E. coli NDH1 shows that two slow- and one fast-relaxing Fe-S clusters become detectable upon reduction by NADH in the presence of OP. However, none of them resembles the mitochondrial cluster 2.

摘要

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