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...

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Bibliographic Details
Published inFEBS letters Vol. 187; no. 2; pp. 253 - 256
Main Authors Chernyak, B.V., Khodjaev, E.Yu, Kozlov, I.A.
Format Journal Article
LanguageEnglish
Published Amsterdam Elsevier 05.08.1985
Subjects
Analytical, structural and metabolic biochemistry
Animals
Biological and medical sciences
Cadmium - pharmacology
Cattle
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
Hydrolases
In Vitro Techniques
Mitochondria, Heart - enzymology
Mitochondrial H+-ATPase
Natural protein inhibitor
Oxidation-Reduction
Proteins - pharmacology
Proton-Translocating ATPases - antagonists & inhibitors
Proton-Translocating ATPases - metabolism
Redox regulation
SH group
Sulfhydryl Compounds
Zinc - pharmacology
Heart
F1-ATPase
Protein inhibitor
Cadmium Ions
Enzyme
Thiohydroxyl group
Zinc Ions
Inactivation
Vertebrata
Mammalia
Oxidation
Artiodactyla
Beef
Ungulata
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Summary: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.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(85)81253-9