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The oxidation of sulfhydryl groups in mitochondrial F 1 ‐ATPase decreases the rate of its inactivation by the natural protein inhibitor
Author(s) -
Chernyak B.V.,
Khodjaev E.Yu.,
Kozlov I.A.
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)81253-9
Subject(s) - submitochondrial particle , chemistry , atpase , divalent , glutathione , biochemistry , inhibitor protein , mitochondrion , enzyme , biophysics , biology , organic chemistry
The oxidants of the SH groups ( o ‐iodozobenzoate, oxidized glutathione, etc.) and the divalent cations of some metals (Zn 2+ and Cd 2+ ) significantly slow down the rate of inactivation by the protein inhibitor of the isolated F 1 ‐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.