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Studies on the proton‐translocating NADH:ubiquinone oxidoreductases of mitochondria and Escherichia coli using the inhibitor 1,10‐phenanthroline
Author(s) -
Finel Moshe,
Majander Anna
Publication year - 1994
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 - 10.1016/0014-5793(94)80402-8
Subject(s) - submitochondrial particle , nadh dehydrogenase , oxidoreductase , escherichia coli , phenanthroline , paracoccus denitrificans , chemistry , mitochondrion , electron transport chain , biochemistry , rotenone , stereochemistry , enzyme , crystallography , protein subunit , gene
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.