The oxidation of sulfhydryl groups in mitochondrial F1-ATPase decreases the rate of its inactivation by the natural protein inhibitor.
The oxidants of the SH groups (o-iodozobenzoate, oxidized glutathione, etc.) and the divalent cations of some metals (Zn2+ and Cd2+) significantly slow down the rate of inactivation by the protein inhibitor of the isolated F1-ATPase and ATPase in submitochondrial particles. Modification of SH groups in the ATPase does not change the rate of inactivation but completely prevents the effect of oxidants.
Chernyak
B V
BV
Khodjaev EYu
Kozlov
I A
IA
D000818:Animals; D002104:Cadmium / Q000494:pharmacology; D002417:Cattle; D066298:In Vitro Techniques; D008929:Mitochondria, Heart / Q000201:enzymology*; D010084:Oxidation-Reduction; D011506:Proteins / Q000494:pharmacology*; D006180:Proton-Translocating ATPases / Q000037:antagonists & inhibitors* / Q000378:metabolism; D013438:Sulfhydryl Compounds; D015032:Zinc / Q000494:pharmacology
D011506:Proteins; D013438:Sulfhydryl Compounds; D002104:Cadmium; D006180:Proton-Translocating ATPases; D015032:Zinc