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

Research output: Contribution to journalArticle

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 languageEnglish
Pages (from-to)8435-8438
Number of pages4
JournalJournal of Physical Chemistry B
Volume113
Issue number25
DOIs
Publication statusPublished - Jun 25 2009

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Propanediol Dehydratase
coenzymes
Coenzymes
mutations
Metal ions
metal ions
Bond length
Binding sites
Binding Sites
Substrates
cobamamide

All Science Journal Classification (ASJC) codes

  • Physical and Theoretical Chemistry
  • Surfaces, Coatings and Films
  • Materials Chemistry

Cite this

What is the identity of the metal ions in the active sites of coenzyme b12-dependent diol dehydratase? a computational mutation analysis. / Kamachi, Takashi; Takahata, Masanori; Toraya, Tetsuo; Yoshizawa, Kazunari.

In: Journal of Physical Chemistry B, Vol. 113, No. 25, 25.06.2009, p. 8435-8438.

Research output: Contribution to journalArticle

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