Abstract
The adenosylcobalamin coenzyme-dependent ethanolamine deaminase from Salmonella typhimurium catalyzes the deamination of aminoethanol to ethanol and ammonia. The product radical observed during steady-state turnover of substrate aminoethanol has been characterized by electron paramagnetic resonance technique. This study explores the conformational dependent hyperfine coupling constants and energetics of the possible product radical intermediates by means of density functional theory based calculations; the results are compared with experimental ones derived from EPR spectra simulations. We have obtained sets of possible conformational structures of the observed product radical indicating that the radical trapped during the catalysis of ethanolamine deaminase corresponds to an activated energy state facilitating the subsequent hydrogen atom abstraction from the inert 5 ′ -methyl group of deoxyadenosine.
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: Physica A: Statistical Mechanics and its Applications
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.
