Evidence for two histidine ligands at the diiron site of methane monooxygenase

D. Drummond, S. SMITH, Howard DALTON

研究成果: Contribution to journalArticle査読

8 被引用数 (Scopus)

抄録

Circular dichroism spectroscopy has shown the hydroxylase component of methane monooxygenase to have a high helical content. The apoprotein has the same secondary structure as the holoenzyme. Chemical modification shows 12 histidines to be reactive with diethylpyrocarbonate in the holoenzyme, whereas 14 are reactive in the apoenzyme. Two histidine residues are implicated as iron ligands. Further chemical modification results suggest a cysteine residue is in close proximity to the diiron centre.

本文言語英語
ページ(範囲)629-633
ページ数5
ジャーナルEuropean Journal of Biochemistry
210
2
DOI
出版ステータス出版済み - 12 1992
外部発表はい

All Science Journal Classification (ASJC) codes

  • 生化学

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