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Acetylene as a suicide substrate and active site probe for methane monooxygenase from Methylococcus capsulatus(Bath)
Open accessAbstract
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.
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Citations
Cited by
Semrau, J. D., DiSpirito, A. A., & Yoon, S. (2010) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2010.00212.x · Cited by 760
Substrate specificity of soluble methane monooxygenase
Green, J., & Dalton, H. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)84627-6 · Cited by 276
Self-citationMembrane-associated methane monooxygenase from Methylococcus capsulatus (Bath)
Zahn, J. A., & DiSpirito, A. A. (1996) · Journal of Bacteriology · doi:10.1128/jb.178.4.1018-1029.1996 · Cited by 256
Hamamura, N., Page, C., Long, T., Semprini, L., & Arp, D. J. (1997) · Applied and Environmental Microbiology · doi:10.1128/aem.63.9.3607-3613.1997 · Cited by 80
Metadata
- Authors
- Prior, S. D., & Dalton, H.
- Venue
- FEMS Microbiology Letters
- Publisher
- Oxford University Press (OUP)
- Published
- 1985-08
- Volume
- 29
- Issue
- 1-2
- Pages
- 105-109
- ISSN
- 0378-1097 (ISSN-L)
- 1574-6968
- OpenAlex
- W2051245368
- Cited by
- 216
- References
- 0
- FWCI
- 1.17
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Prior, S. D., & Dalton, H. (1985). Acetylene as a suicide substrate and active site probe for methane monooxygenase from Methylococcus capsulatus(Bath). FEMS Microbiology Letters. https://doi.org/10.1111/j.1574-6968.1985.tb00843.x
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