Inhibition of electron transport of rat liver mitochondria by unnatural (-)-antimycin A3.
The inhibition of electron transport by unnatural (-)-antimycin A3 was examined with rat liver mitochondria and compared with that of natural (+)-antimycin A3. (-)-Antimycin A3 inhibited respiration about 1/100th as strongly as natural (+)-antimycin A3. (-)-Antimycin A3 binding to the cytochrome bc1 complex did not seem to induce a conformational change in this proteinous complex. The binding site of (-)-antimycin A3 was probably the same as that of (+)-antimycin A3 (at the Qi center). However, the mode of interaction with the Qi center by (-)-antimycin A3 and (+)-antimycin A3 was somewhat different.
Miyoshi
H
H
Department of Agricultural Chemistry, Kyoto University, Japan.
Kondo
H
H
Oritani
T
T
Saitoh
I
I
Iwamura
H
H
D000818:Animals; D000968:Antimycin A / Q000378:metabolism / Q000494:pharmacology*; D001665:Binding Sites; D003573:Cytochrome b Group / Q000378:metabolism; D004579:Electron Transport; D008930:Mitochondria, Liver / Q000187:drug effects* / Q000378:metabolism; D010084:Oxidation-Reduction; D051381:Rats; D013057:Spectrum Analysis; D013237:Stereoisomerism; D013386:Succinates / Q000494:pharmacology; D019802:Succinic Acid
D003573:Cytochrome b Group; D013386:Succinates; D000968:Antimycin A; D019802:Succinic Acid