Acetylene as a suicide substrate and active site probe for methane monooxygenase from Methylococcus capsulatus (Bath)
Year: 1985
Type: article
Abstract: Acetylene was shown to be an inhibitor of cell-free methane monooxygenase (MMO) activity in Methylococcus capsulatus (Bath). Inhibition was demonstrated for both the soluble and particulate forms of the enzyme and was dependent on the presence of both NADH and oxygen. Inactivation of the enzyme complex was irreversible and was due to binding of the acetylene to specific proteins of the enzyme complex. The use of radiolabelled [14C]acetylene provided a method for visualisation of the bound inhibitor: protein complex on sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (PAGE). Acetylene was shown to bind to proteins which are associated with methane-oxidising activity and it is proposed that acetylene acts as a suicide substrate.
Source: FEMS Microbiology Letters
Authors: S.D. Prior, H. Dalton
Institution: University of Warwick
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: bronze
OpenAlex ID: W2051245368