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

FEBS Letters

Finel, Moshe¹  Majander, Anna¹ 

[1] Helsinki Bioenergetics Group, Department of Medical Chemistry, PO Box 8, University of Helsinki, 00140 Helsinki, Finland

关键词: Orthophenantroline;    Iron-sulfur cluster;    NADH dehydrogenase;    Bacterial NDH1;    Mitochondrial complex I;    DB;    2;    3-dimethoxy-5-methyl-6-n-decyl-1;    4-benzoquinone;    EPR;    electron paramagnetic resonance;    OP;    1;    10-phenanthroline (orthophenanthroline);    PMSF;    phenylmethylsulfonyl fluoride;    SMP;    submitochondrial particles;   

DOI  :  10.1016/0014-5793(94)80402-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown