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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.

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, with linear regions over 295 → 220 K (monoexponential) and 214 → 203 K (biexponential) that are delineated by a kinetic bifurcation and kinks at 219 and 217 K, respectively. The results are interpreted by using a free energy landscape model and derived microscopic kinetic mechanism. The bifurcation and kink transitions correspond to the effective quenching of two distinct sets of native collective protein configurational fluctuations that (1) reconfigure the protein within the substrate radical free ene

SUBMITTER: Kohne M

PROVIDER: S-EPMC5585081 | biostudies-literature | 2017 Jun

REPOSITORIES: biostudies-literature

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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.

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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.

OmicsDI is part of the ELIXIR infrastructure

Tweets

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.