Two Dynamical Regimes of the Substrate Radical Rearrangement Reaction in B12-Dependent Ethanolamine Ammonia-Lyase Resolve Contributions of Native Protein Configurations and Collective Configurational Fluctuations to Catalysis.
Sign Up to like & getrecommendations! Published in 2017 at "Biochemistry"
DOI: 10.1021/acs.biochem.7b00294
Abstract: The kinetics of the substrate radical rearrangement reaction step in B12-dependent ethanolamine ammonia-lyase (EAL) from Salmonella typhimurium are measured over a 92 K temperature range. The observed first-order rate constants display a piecewise-continuous Arrhenius dependence,… read more here.
Keywords: rearrangement reaction; substrate radical; radical rearrangement; reaction ... See more keywords
Deuterium Kinetic Isotope Effects Resolve Low-Temperature Substrate Radical Reaction Pathways and Steps in B12-Dependent Ethanolamine Ammonia-Lyase.
Sign Up to like & getrecommendations! Published in 2019 at "Biochemistry"
DOI: 10.1021/acs.biochem.9b00588
Abstract: The first-order reaction kinetics of the cryotrapped 1,1,2,2-2H4-aminoethanol substrate radical intermediate state in the adenosylcobalamin (B12)-dependent ethanolamine ammonia-lyase (EAL) from Salmonella enterica serovar Typhimurium are measured over the range of 203-225 K by using time-resolved,… read more here.
Keywords: substrate radical; reaction; b12 dependent; ethanolamine ammonia ... See more keywords
Mechanism of Light Induced Radical Pair Formation in Coenzyme B12-Dependent Ethanolamine Ammonia-Lyase
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DOI: 10.1021/acscatal.8b00120
Abstract: Coenzyme B12 (adenosylcobalamin = AdoCbl)-dependent enzymes catalyze complex molecular transformations by employing radical chemistry. The initial step in the native catalytic cycle, upon substrate binding, involves homolytic cleavage of the Co–C bond of AdoCbl to… read more here.
Keywords: coenzyme b12; radical pair; mechanism; ethanolamine ammonia ... See more keywords