EVIDENCE FOR 2 HISTIDINE LIGANDS AT THE DIIRON SITE OF METHANE MONOOXYGENASE

被引:6
作者
DRUMMOND, D [1 ]
SMITH, S [1 ]
DALTON, H [1 ]
机构
[1] UNIV WARWICK,DEPT BIOL SCI,COVENTRY CV4 7AL,W MIDLANDS,ENGLAND
来源
EUROPEAN JOURNAL OF BIOCHEMISTRY | 1992年 / 210卷 / 02期
关键词
D O I
10.1111/j.1432-1033.1992.tb17463.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:629 / 633
页数:5
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