Open AccessEvidence for two histidine ligands at the diiron site of methane monooxygenase
Author(s) -
Drummond D.,
SMITH S.,
DALTON Howard
Publication year - 1992
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1992.tb17463.x
Subject(s) - methane monooxygenase , histidine , chemistry , residue (chemistry) , circular dichroism , monooxygenase , cysteine , chemical modification , enzyme , stereochemistry , active site , methane , biochemistry , organic chemistry , cytochrome p450
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.