Year-end Sale % OFF 
Abstract
Soluble guanylate cyclase (sGC) is the most important receptor for the signaling molecule NO. NO activates sGC by binding to its heme cofactor and reacts with free thiols in the protein itself. The S-nitrosation of cysteine thiols affects the activity of soluble guanylate cyclase (sGC). In this study, infrared (IR) spectroscopy and site-directed mutagenesis were used to investigate S–H vibration and the process of S-nitrosation in the β1 subunit (amino acids 1–194) of sGC. Fourier transform IR spectroscopy revealed that wild-type and mutants (C78S and C122S) of sGC β1(1–194) exhibited S–H peaks around 2560cm−1. The signals were attenuated in the IR spectra of S-nitrosoglutathione-treated mutants, demonstrating that S-nitrosation in sGC β1(1–194) occured at residues C78 and C122, and the process of the reaction was GSNO concentration-dependent.
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.
