Acetylene as a suicide substrate and active site probe for methane monooxygenase from Methylococcus capsulatus (Bath)
- S. D. Prior, H. Dalton
- Biology, Chemistry
- 1 August 1985
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.
The soluble methane mono-oxygenase of Methylococcus capsulatus (Bath). Its ability to oxygenate n-alkanes, n-alkenes, ethers, and alicyclic, aromatic and heterocyclic compounds.
- J. Colby, D. Stirling, H. Dalton
- Chemistry, BiologyBiochemical Journal
- 1 August 1977
Methane mono-oxygenase of Methylococcus capsulatus (Bath) catalyses the oxidation of various substituted methane derivatives including methanol and, in some of its catalytic properties, apparently resembles the analogous enzyme from Methylomonas methanica but differs from those found in Methylosinus trichosporium and M methylomonas albus.
Copper stress underlies the fundamental change in intracellular location of methane mono-oxygenase in methane-oxidizing organisms: Studies in batch and continuous cultures
- S. H. Stanley, S. Prior, D. Leak, H. Dalton
- BiologyBiotechnology Letters
- 2004
Results indicated that the copper effect could explain a similar switch in intracellular location observed in Methylosinus trichosporium OB3b but that some methanotrophs do not have the capacity to overcome copper stress in this way.
The membrane-associated form of methane mono-oxygenase from Methylococcus capsulatus (Bath) is a copper/iron protein.
- P. Basu, B. Katterle, K. Andersson, H. Dalton
- BiologyBiochemical Journal
- 15 January 2003
The essential role of copper in enzyme catalysis is verified, the implausibility of copper existing as a trinuclear cluster is indicated and the presence of a tightly bound mononuclear Fe(3+) ion in an octahedral environment that may well be exchange-coupled to another paramagnetic species is demonstrated.
The effect of copper ions on membrane content and methane monooxygenase activity in methanol-grown cells of Methylococcus capsulatus (Bath)
- S. D. Prior, H. Dalton
- Biology
- 1985
Cells grown on methanol exhibited differences in methane monooxygenase (MMO) activity which were dependent on the concentration of copper sulphate present in the growth medium, which enhanced both in vivo and in vitro MMO activity.
Nitrogen Fixation in Obligate Methanotrophs
- J. Murrell, H. Dalton
- Biology
- 1 November 1983
A number of representative species of obligate methane-oxidizing bacteria were surveyed for their ability to fix N2 by growth experiments and the acetylene reduction test and only type II organisms and the type X methanotroph Methylococcus capsulatus (Bath) grew well in nitrogen-free liquid medium and were capable of active acetylene Reduction.
The Methylotrophic Bacteria
- R. Whittenbury, H. Dalton
- Biology
- 1981
Three groups of microbes are considered here: the methane utilizer, the methanol utilizers, and the carbon monoxide utilizers; these appear to be composed of distinctive groups of bacteria with properties that set them apart from the majority of other microbes.
Enantioselective bacterial biotransformation routes to cis-diol metabolites of monosubstituted benzenes, naphthalene and benzocycloalkenes of either absolute configuration
- C. Allen, D. Boyd, S. C. Taylor
- Chemistry, Biology
- 1995
Enzyme-catalysed kinetic resolution and asymmetric dihydroxylation routes to enantiopure cis-diol metabolites of arenes and benzocycloalkenes of either absolute configuration have been developed…
The methane monooxygenase gene cluster of Methylococcus capsulatus (Bath).
- A. Stainthorpe, V. Lees, G. Salmond, H. Dalton, J. Murrell
- BiologyGene
- 1990
The Leeuwenhoek Lecture 2000 The natural and unnatural history of methane-oxidizing bacteria
- H. Dalton
- Biology, ChemistryPhilosophical Transactions of the Royal Society B…
- 29 June 2005
Understanding of how bacteria are capable of effecting one of the most difficult reactions in chemistry—namely, the controlled oxidation of methane to methanol—has been made possible by the isolation, in pure form, of the enzyme components.
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