Interaction of rhodanese with intermediates of oxygen reduction

FEBS Letters

D'Ottavio, Palmerino¹  Cannella, Carlo²  Berni, Rodolfo² 

[1] Institute of Biological Chemistry, ‘La Sapienza’ University of Rome, P.1e A. Moro 5, 00185 Rome, Italy;Institutes of Biochemistry and Molecular Biology, University of Parma, Via del Taglio, 43100 Parma Italy

关键词: Rhodanese;    Phenylglyoxal;    Cyanide;    Thiosulfate;    Superoxide radical;    Hydrogen peroxide;   

DOI  :  10.1016/0014-5793(83)81074-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Cyanide-promoted inactivation of the enzyme rhodanese [thiosulfate sulfurtransferase (EC 2.8.1.1)] in the presence of ketoaldehydes is caused by reduced forms of molecular oxygen generated during autoxidation of the reaction products. The requirement of both catalase and superoxide dismutase to prevent rhodanese inactivation indicates that hydroxyl radical could be the most efficient inactivating agent. Rhodanese, also in the less stable sulfur-free form, shows a different sensitivity towards oxygen activated species. While the enzyme is unaffected by superoxide radical, it is rapidly inactivated by hydrogen peroxide. The extent of inactivation depends on the molar ratio between sulfur-free enzyme and oxidizing agent. Fully inactive enzyme is reactivated by reduction with its substrate thiosulfate.

【 授权许可】

Unknown