Abstract
Reactions of the selective inorganic radical anions (SCN)–2 and Br–2, with subtilisins Novo and Carlsberg lead to selective oxidation of the tryptophan, tyrosine, and histidine amino-acid residues. Inactivation studies show that most of the inactivation is caused by oxidation of one or more histidine residues. Oxidation of tryptophan residues has a minor effect upon activity but damage to tyrosine residues does not affect the activity of the two enzymes towards the small synthetic substrate N-acetyl-L-tyrosine ethyl ester. Rate constants for reactions with the radical anions and transient spectra, measured by pulse radiolysis, reflect the differences in amino-acid composition and in structure between the two enzymes.
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 callMore From: Journal of the Chemical Society, Faraday Transactions 1: Physical Chemistry in Condensed Phases
Disclaimer: 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.
