Glutamate 338 is an electrostatic facilitator of C-Co bond breakage in a dynamic/electrostatic model of catalysis by ornithine aminomutase.

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Glutamate 338 is an electrostatic facilitator of C-Co bond breakage in a dynamic/electrostatic model of catalysis by ornithine aminomutase.

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Glutamate 338 is an electrosta ...... ysis by ornithine aminomutase.

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Glutamate 338 is an electrosta ...... ysis by ornithine aminomutase.

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Glutamate 338 is an electrosta ...... ysis by ornithine aminomutase.

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P1476

Glutamate 338 is an electrosta ...... ysis by ornithine aminomutase.

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P2093

Binuraj R K Menon

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David Leys

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Karl Fisher

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Navya Menon

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Stephen E J Rigby

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P2860

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The crystal structure of coenzyme B12-dependent glycerol dehydratase in complex with cobalamin and propane-1,2-diol

Substrate-induced conformational change of a coenzyme B12-dependent enzyme: crystal structure of the substrate-free form of diol dehydratase

Large-scale Domain Dynamics and Adenosylcobalamin Reorientation Orchestrate Radical Catalysis in Ornithine 4,5-Aminomutase

Structures of the Human GTPase MMAA and Vitamin B 12 -dependent Methylmalonyl-CoA Mutase and Insight into Their Complex Formation

Characterization of protein contributions to cobalt-carbon bond cleavage catalysis in adenosylcobalamin-dependent ethanolamine ammonia-lyase by using photolysis in the ternary complex.

Molecular modeling of the mechanochemical triggering mechanism for catalysis of carbon-cobalt bond homolysis in coenzyme B12.

The role of solvent viscosity in the dynamics of protein conformational changes.

Mutagenesis alters the catalytic mechanism of the light-driven enzyme protochlorophyllide oxidoreductase

Adenosyl radical: reagent and catalyst in enzyme reactions.

P304

1242-1255

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P31

scholarly article

P356

10.1111/FEBS.13215

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P407

English

P433

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P478

282

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P50

Nigel Scrutton

P577

2015-02-12T00:00:00Z

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P698

25627283

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P932

4413051

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