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

Yoko Katayama*, Kanako Hashimoto, Hiroshi Nakayama, Hiroyuki Mino, Masaki Nojiri, Taka Aki Ono, Hiroshi Nyunoya, Masafumi Yohda, Koji Takio, Masafumi Odaka

*この研究の対応する著者

研究成果: Article査読

41 被引用数 (Scopus)

抄録

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.

本文言語English
ページ(範囲)728-729
ページ数2
ジャーナルJournal of the American Chemical Society
128
3
DOI
出版ステータスPublished - 2006 1 25
外部発表はい

ASJC Scopus subject areas

  • 触媒
  • 化学 (全般)
  • 生化学
  • コロイド化学および表面化学

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