Comparison of HydSl Hydrogenase of  Thiocapsa bogorovii  and its Modification with Truncated C-terminus of HydS

A. S. Starodubov; Стародубов А. С.; M. K. Khasimov; Хасимов М. Х.; A. N. Khusnutdinova; Хустнутдинова А. Н.; N. A. Zorin; Зорин Н. А.; A. A. Tsygankov; Цыганков А. А.

doi:10.31857/S0555109923040141

Comparison of HydSl Hydrogenase of Thiocapsa bogorovii and its Modification with Truncated C-terminus of HydS

Authors: Starodubov A.S.¹, Khasimov M.K.¹, Khusnutdinova A.N.¹, Zorin N.A.¹, Tsygankov A.A.¹
Affiliations:
1. Institute of Basic Biological Problems of the Russian Academy of Sciences
Issue: Vol 59, No 5 (2023)
Pages: 450-456
Section: Articles
URL: https://cardiosomatics.ru/0555-1099/article/view/674597
DOI: https://doi.org/10.31857/S0555109923040141
EDN: https://elibrary.ru/QZNSAD
ID: 674597

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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.

Keywords

HydSL hydrogenase, Thiocapsa bogorovii, C-terminal fragment of HydS, modified HydSL hydrogenase, thermal stability, hydrogen, silver nitrate, hydrogenase

References

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