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

Douglas Robert Drummond, S. SMITH, Howard DALTON

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)629-633
Number of pages5
JournalEuropean Journal of Biochemistry
Volume210
Issue number2
DOIs
Publication statusPublished - Jan 1 1992

Fingerprint

methane monooxygenase
Holoenzymes
Chemical modification
Histidine
Diethyl Pyrocarbonate
Circular dichroism spectroscopy
Ligands
Apoenzymes
Apoproteins
Circular Dichroism
Mixed Function Oxygenases
Cysteine
Spectrum Analysis
Iron

All Science Journal Classification (ASJC) codes

  • Biochemistry

Cite this

Evidence for two histidine ligands at the diiron site of methane monooxygenase. / Drummond, Douglas Robert; SMITH, S.; DALTON, Howard.

In: European Journal of Biochemistry, Vol. 210, No. 2, 01.01.1992, p. 629-633.

Research output: Contribution to journalArticle

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