Affiliation:
1. Institute of Basic Biological Problems of the Russian Academy of Sciences
Abstract
Native HydSL hydrogenase of Thiocapsa bogorovii and its modification with truncated C-terminus of HydS (delta54HydS) were shown to be similar in specific activity, thermostability and temperature dependence of activity. It supports the suggestion that C-terminus of HydS does not participate in stabilization of the enzyme structure. Ag+ ions irreversibly inactivated both hydrogenases but delta54HydS was more sensitive to this inhibitor. In the presence of Ag+ the absorption peak at 410 nm was bleached indicating the destruction of FeS clusters. Protein globule was also destructed by Ag+. Prolonged incubation of hydrogenase with Ag+ ions led to disappearance of CO and CN peaks in IR spectra indicating NiFe center impairment. Data suggest that the first target of Ag+ ions is distal FeS cluster, and C-terminus of HydS interacts with Ag+ decreasing local ion concentration near the distal FeS cluster.
Publisher
The Russian Academy of Sciences
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