Inactivation of mitochondrial ATPase by ultraviolet light.
The present work describes experiments that show that far-ultraviolet irradiation induce the inhibition of ATPase activity in both membrane-bound and soluble F1. It was also found that ultraviolet light promotes the release of tightly bound adenine nucleotides from F1-ATPase. Experiments carried out with submitochondrial particles indicate that succinate partially protects against these effects of ultraviolet light. Titration of sulfhydryl groups in both irradiated submitochondrial particles and soluble F1-ATPase indicates that a conformational change induced by photochemical modifications of amino acid residues appears involved in the inactivation of the enzyme. Finally, experiments are described which show that the tyrosine residue located in the active site of F1-ATPase is modified by ultraviolet irradiation.
D000251:Adenosine Triphosphatases / Q000528:radiation effects*; D000818:Animals; D002417:Cattle; D055598:Chemical Phenomena; D002621:Chemistry; D066298:In Vitro Techniques; D008929:Mitochondria, Heart / Q000201:enzymology*; D011485:Protein Binding; D006180:Proton-Translocating ATPases / Q000528:radiation effects; D012995:Solubility; D014443:Tyrosine / Q000302:isolation & purification; D014466:Ultraviolet Rays
D014443:Tyrosine; D000251:Adenosine Triphosphatases; D006180:Proton-Translocating ATPases