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Title: Cysteine 295 indirectly affects Ni coordination of carbon monoxide dehydrogenase-II C-cluster

Highlights: •CODH-II harbors a unique [Ni-Fe-S] cluster. •We substituted the ligand residues of Cys{sup 295} and His{sup 261}. •Dramatic decreases in Ni content upon substitutions were observed. •All substitutions did not affect Fe-S clusters assembly. •CO oxidation activity was decreased by the substitutions. -- Abstract: A unique [Ni–Fe–S] cluster (C-cluster) constitutes the active center of Ni-containing carbon monoxide dehydrogenases (CODHs). His{sup 261}, which coordinates one of the Fe atoms with Cys{sup 295}, is suggested to be the only residue required for Ni coordination in the C-cluster. To evaluate the role of Cys{sup 295}, we constructed CODH-II variants. Ala substitution for the Cys{sup 295} substitution resulted in the decrease of Ni content and didn’t result in major change of Fe content. In addition, the substitution had no effect on the ability to assemble a full complement of [Fe–S] clusters. This strongly suggests Cys{sup 295} indirectly and His{sup 261} together affect Ni-coordination in the C-cluster.
Authors:
; ;  [1] ;  [2] ; ;  [1] ;  [3] ;  [1]
  1. Division of Applied Biosciences, Graduate School of Agriculture, Kyoto University, Kyoto 606-8502 (Japan)
  2. Organization for Promotion of Tenure Track, University of Miyazaki, Miyazaki 889-1692 (Japan)
  3. Department of Biological Sciences, Graduate School of Science, Osaka University, Toyonaka, Osaka 560-0043 (Japan)
Publication Date:
OSTI Identifier:
22242175
Resource Type:
Journal Article
Resource Relation:
Journal Name: Biochemical and Biophysical Research Communications; Journal Volume: 441; Journal Issue: 1; Other Information: Copyright (c) 2013 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; CARBON MONOXIDE; COENZYMES; COMPLEMENT; CYSTEINE; HYDROXYLAMINE; OXIDATION; OXIDOREDUCTASES; POLYMERASE CHAIN REACTION