What is the identity of the metal ions in the active sites of coenzyme B12-dependent diol dehydratase? A computational mutation analysis.

Takashi Kamachi, Masanori Takahata, Tetsuo Toraya, Kazunari Yoshizawa

Journal: The journal of physical chemistry. B 2009;113(25):8435-8

PMID: 19338314

Full Text on American Chemical Society View on PubMed

Abstract

What is the identity of the metal ion in the active sites of diol dehydratase? To address this question, we calculated the M-O bond lengths in the active sites using QM/MM calculations (M=K, Na, Mg, Ca). Our results show that the previous assignment of the metal ion in the substrate-binding site is wrong and that the identity of the metal ion is likely to be Ca2+. This is consistent with accumulated experimental evidence.

DOI: 10.1021/jp9001737

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https://doi.org/10.1021/jp9001737

MeSH Terms: Catalytic Domain, Cobamides, Computer Simulation, Metals, Models, Molecular, Mutation, Propanediol Dehydratase, Quantum Theory