The Library
EVIDENCE FOR 2 HISTIDINE LIGANDS AT THE DIIRON SITE OF METHANE MONOOXYGENASE
Tools
UNSPECIFIED (1992) EVIDENCE FOR 2 HISTIDINE LIGANDS AT THE DIIRON SITE OF METHANE MONOOXYGENASE. EUROPEAN JOURNAL OF BIOCHEMISTRY, 210 (2). pp. 629-633. ISSN 0014-2956.
Research output not available from this repository.
Request-a-Copy directly from author or use local Library Get it For Me service.
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.
Item Type: | Journal Article | ||||
---|---|---|---|---|---|
Subjects: | Q Science > QD Chemistry | ||||
Journal or Publication Title: | EUROPEAN JOURNAL OF BIOCHEMISTRY | ||||
Publisher: | SPRINGER VERLAG | ||||
ISSN: | 0014-2956 | ||||
Official Date: | 1 December 1992 | ||||
Dates: |
|
||||
Volume: | 210 | ||||
Number: | 2 | ||||
Number of Pages: | 5 | ||||
Page Range: | pp. 629-633 | ||||
Publication Status: | Published |
Data sourced from Thomson Reuters' Web of Knowledge
Request changes or add full text files to a record
Repository staff actions (login required)
View Item |