Jump to main content
Jump to site search
PLANNED MAINTENANCE Close the message box

Scheduled maintenance upgrade on Thursday 4th of May 2017 from 8.00am to 9.00am (BST).

During this time our websites will be offline temporarily. If you have any questions please use the feedback button on this page. We apologise for any inconvenience this might cause and thank you for your patience.


Issue 21, 1997
Previous Article Next Article

Principles of small molecule activation by metalloenzymes as exemplified by the soluble methane monooxygenase from Methylococcus capsulatus (Bath) *

Abstract

Many metalloenzymes activate small molecules in a manner that is unique to natural systems. In this Perspective we discuss the soluble methane monooxygenase protein system from Methylococcus capsulatus (Bath), which uses a mixed-function oxidase to convert methane selectively to methanol. Through a series of biophysical studies, theoretical calculations, synthetic model studies and mechanistic biochemical experiments, the respective roles of the carboxylate-bridged non-heme diiron center and the protein environment in controlling the enzyme mechanism have been delineated. These results are used to identify themes common among metalloenzymes that activate small molecules and to identify future directions for the study of this protein system.

Back to tab navigation
Please wait while Download options loads

Article type: Paper
DOI: 10.1039/A705116F
Citation: J. Chem. Soc., Dalton Trans., 1997, 3925-3932
  •   Request permissions

    Principles of small molecule activation by metalloenzymes as exemplified by the soluble methane monooxygenase from Methylococcus capsulatus (Bath) *

    A. M. Valentine and S. J. Lippard, J. Chem. Soc., Dalton Trans., 1997, 3925
    DOI: 10.1039/A705116F

Search articles by author