Cysteine 295 indirectly affects Ni coordination of carbon monoxide dehydrogenase-II C-cluster.
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抄録
A unique [Ni-Fe-S] cluster (C-cluster) constitutes the active center of Ni-containing carbon monoxide dehydrogenases (CODHs). His(261), which coordinates one of the Fe atoms with Cys(295), is suggested to be the only residue required for Ni coordination in the C-cluster. To evaluate the role of Cys(295), we constructed CODH-II variants. Ala substitution for the Cys(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(295) indirectly and His(261) together affect Ni-coordination in the C-cluster.
収録刊行物
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- Biochemical and biophysical research communications
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Biochemical and biophysical research communications 441 (1), 13-17, 2013-11-08
Elsevier Inc.
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詳細情報 詳細情報について
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- CRID
- 1050282810757251968
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- NII論文ID
- 120005357089
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- NII書誌ID
- AA00564395
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- ISSN
- 0006291X
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- HANDLE
- 2433/179795
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- 本文言語コード
- en
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- 資料種別
- journal article
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- データソース種別
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- IRDB
- CiNii Articles