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

D. Drummond; S. SMITH; Howard DALTON

doi:10.1111/j.1432-1033.1992.tb17463.x

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

D. Drummond, S. SMITH, Howard DALTON

Research output: Contribution to journal › Article › peer-review

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 language	English
Pages (from-to)	629-633
Number of pages	5
Journal	European Journal of Biochemistry
Volume	210
Issue number	2
DOIs	https://doi.org/10.1111/j.1432-1033.1992.tb17463.x
Publication status	Published - Dec 1992
Externally published	Yes

All Science Journal Classification (ASJC) codes

Biochemistry

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10.1111/j.1432-1033.1992.tb17463.x

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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.",

author = "D. Drummond and S. SMITH and Howard DALTON",

year = "1992",

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AU - Drummond, D.

AU - SMITH, S.

AU - DALTON, Howard

PY - 1992/12

Y1 - 1992/12

N2 - 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.

AB - 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.

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

Abstract

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