Thiocyanate hydrolase is a cobalt-containing metalloenzyme with a cysteine-sulfinic acid ligand

被引:49
作者
Katayama, Y [1 ]
Hashimoto, K
Nakayama, H
Mino, H
Nojiri, M
Ono, T
Nyunoya, H
Yohda, M
Takio, K
Odaka, M
机构
[1] Tokyo Univ Agr & Technol, Grad Sch Agr, Dept Environm & Nat Resource Sci, Fuchu, Tokyo 1838509, Japan
[2] Tokyo Univ Agr & Technol, Ctr Gene Res, Fuchu, Tokyo 1838509, Japan
[3] Tokyo Univ Agr & Technol, Grad Sch Technol, Dept Biotechnol & Life Sci, Koganei, Tokyo 1848588, Japan
[4] Nagoya Univ, Grad Sch Sci, Div Sci Mat Phys, Nagoya, Aichi 4648602, Japan
[5] Osaka Univ, Grad Sch Sci, Toyonaka, Osaka 5600043, Japan
[6] RIKEN, Biomol Characterizat Team, Wako, Saitama 3510198, Japan
[7] RIKEN, Mol Membranes Biol Lab, Wako, Saitama 3510198, Japan
[8] RIKEN, Harima Inst, Biomet Sci Lab, Sayo, Hyogo 6795148, Japan
关键词
D O I
10.1021/ja057010q
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Thiocyanate hydrolase (SCNase) purified from Thiobacillus thioparus THI115 hydrolyzes thiocyanate to carbonyl sulfide and ammonia. DNA sequences of the cloned genes revealed the close relation of SCNase to nitrile hydratase (NHase). The consensus sequences for coordination of the metal ion found in NHases were also conserved in the γ subunit of SCNase. Here, we showed that the SCNase contained one cobalt atom per αβγ heterotrimer. UV-vis absorption spectrum suggested that the cobalt exists as a non-corrin ion. Reduced SCNase showed an ESR signal characteristic of low-spin Co2+, which closely resembled that of the Co-type NHases. Mass spectrometry for the peptide fragment containing the metal-binding motif of the SCNase γ subunit indicated that the cysteine residue at position 131 was post-translationally oxidized to a cysteine-sulfinic acid. From these results, we concluded that SCNases and NHases form a novel non-corrin and/or non-heme protein family having post-translationally modified cysteine ligands. Copyright © 2006 American Chemical Society.
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收藏
页码:728 / 729
页数:2
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