Cysteine 295 indirectly affects Ni coordination of carbon monoxide dehydrogenase-II C-cluster
Cysteine 295 indirectly affects Ni coordination of carbon monoxide dehydrogenase-II C-cluster
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DOI：
10.1016/j.bbrc.2013.09.143
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发表时间：
2013-11-08
影响因子：
3.1
通讯作者：
Sako, Yoshihiko
中科院分区：
文献类型：
--
作者：
Inoue, Takahiro;Takao, Kyosuke;Sako, Yoshihiko
一个独特的[Ni-Fe-S]簇（C簇）构成了含镍一氧化碳脱氢酶（CODH）的活性中心。His（261）与Cys（295）配位，是C簇中Ni配位所需的唯一残基。为了评估Cys（295）的作用，我们构建了CODH-II变体。Ala取代Cys（295）导致Ni含量降低，而Fe含量变化不大。此外，取代对组装完整[Fe-S]簇的能力没有影响。这强烈表明Cys（295）间接地和His（261）一起影响C簇中的Ni配位。(C)2013 Elsevier Inc.版权所有© 2016
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. (C) 2013 Elsevier Inc. All rights reserved..