EPR studies of the possible binding sites of the cluster N2, semiquinones, and specific inhibitors of the NADH:quinone oxidoreductase (complex I).
Ohnishi
T
T
Johnson Research Foundation and Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia 19104, USA.
Magnitsky
S
S
Toulokhonova
L
L
Yano
T
T
Yagi
T
T
Burbaev
D S
DS
Vinogradov
A D
AD
Sled
V D
VD
D000818:Animals; D001665:Binding Sites; D004305:Dose-Response Relationship, Drug; D004578:Electron Spin Resonance Spectroscopy / Q000379:methods; D004926:Escherichia coli / Q000201:enzymology; D007425:Intracellular Membranes / Q000378:metabolism; D008928:Mitochondria / Q000378:metabolism; D008954:Models, Biological; D011808:Quinone Reductases / Q000037:antagonists & inhibitors* / Q000737:chemistry*; D012402:Rotenone / Q000494:pharmacology; D014475:Uncoupling Agents / Q000494:pharmacology
D014475:Uncoupling Agents; D012402:Rotenone; C041831:NADH dehydrogenase (quinone); D011808:Quinone Reductases