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Title: Cysteine 295 indirectly affects Ni coordination of carbon monoxide dehydrogenase-II C-cluster.
Authors: Inoue, Takahiro
Takao, Kyosuke
Yoshida, Takashi  kyouindb  KAKEN_id
Wada, Kei
Daifuku, Takashi
Yoneda, Yasuko
Fukuyama, Keiichi
Sako, Yoshihiko  kyouindb  KAKEN_id
Author's alias: 左子, 芳彦
Keywords: Carbon monoxide dehydrogenase
[Ni–Fe–S] cluster
Carboxydothermus hydrogenoformans
Issue Date: 8-Nov-2013
Publisher: Elsevier Inc.
Journal title: Biochemical and biophysical research communications
Volume: 441
Issue: 1
Start page: 13
End page: 17
Abstract: 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.
Rights: © 2013 Elsevier Inc.
This is not the published version. Please cite only the published version. この論文は出版社版でありません。引用の際には出版社版をご確認ご利用ください。
DOI(Published Version): 10.1016/j.bbrc.2013.09.143
PubMed ID: 24120497
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