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

doi:10.1021/jp9001737

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

Department of Fundamental Organic Chemistry

Research output: Contribution to journal › Article › peer-review

14 Citations (Scopus)

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.

Original language	English
Pages (from-to)	8435-8438
Number of pages	4
Journal	Journal of Physical Chemistry B
Volume	113
Issue number	25
DOIs	https://doi.org/10.1021/jp9001737
Publication status	Published - Jun 25 2009

All Science Journal Classification (ASJC) codes

Physical and Theoretical Chemistry
Surfaces, Coatings and Films
Materials Chemistry

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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.",

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AU - Yoshizawa, Kazunari

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What is the identity of the metal ions in the active sites of coenzyme b12-dependent diol dehydratase? a computational mutation analysis

Abstract

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