Abstract
The inhibitory effect of mercury(II) chloride on the activity and structure of the hydrogenase Thiocapsa roseopersicina BBS was studied. The kinetics of hydrogenase inactivation in the presence of different inhibitor concentrations was determined. The irreversible nature of Hg²⁺ action was established, and hydrogenase inhibition constants at different temperatures were determined. The presence of this inhibitor in enzyme solution significantly reduced its stability and caused denaturation at temperatures above 50°C. In the process of enzyme incubation with Hg²⁺, the absorption band fades in the visible region of the spectrum, indicating the destruction of iron–sulfur clusters. Comparative analysis of the infrared Fourier spectra of hydrogenase without the addition and after incubation with inhibitor indicates the destruction of the NiFe active center.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
