X-ray crystal structure of Escherichia coli taurine/alpha-ketoglutarate dioxygenase complexed to ferrous iron and substrates.
- J. Elkins, M. J. Ryle, P. Roach
- Biology, ChemistryBiochemistry
- 23 April 2002
The TauD structure and TfdA model define the metal ligands and the positions of nearby aromatic residues that undergo post-translational modifications involving self-hydroxylation reactions, providing insight into the mechanism of enzyme catalysis.
Heterologous expression of soluble methane monooxygenase genes in methanotrophs containing only particulate methane monooxygenase
- J. S. Lloyd, P. De Marco, H. Dalton, J. Murrell
- Biology, EngineeringArchives of Microbiology
- 1 May 1999
Abstract The methanotrophs Methylococcus capsulatus (Bath) and Methylosinus trichosporium OB3b contain particulate methane monooxygenase (pMMO) and soluble methane monooxygenase (sMMO) genes. Other…
Heterologous expression of alkene monooxygenase from Rhodococcus rhodochrous B-276.
- T. Smith, J. S. Lloyd, S. C. Gallagher, W. Fosdike, J. Murrell, H. Dalton
- BiologyEuropean Journal of Biochemistry
- 25 December 2001
The expression systems described here now allow structure/function studies on AMO to be carried out by site-directed mutagenesis.
Inactivation of the regulatory protein B of soluble methane monooxygenase from Methylococcus capsulatus (Bath) by proteolysis can be overcome by a Gly to Gln modification.
- J. S. Lloyd, A. Bhambra, J. Murrell, H. Dalton
- BiologyEuropean Journal of Biochemistry
- 1 August 1997
The amount of active protein B present in the cell may be controlled by protein B cleavage, thereby regulating electron transfer and this may control the activity of sMMO in response to the supply of methane to the cell.
Homologous expression of soluble methane monooxygenase genes in Methylosinus trichosporium OB3b.
- J. S. Lloyd, R. Finch, H. Dalton, J. Murrell
- BiologyMicrobiology
- 1 February 1999
This is the first report of homologous sMMO expression in a methanotroph with enzyme activities that are comparable to the activity reported in wild-type strains.
Heterologous expression and site-directed mutagenesis of soluble methane monooxygenase.
- J. S. Lloyd
- Biology
- 1 November 1997
The purpose of this investigation was to study the heterologous expression of soluble methane monooxygenase (sMMO) genes from Methylococcus capsulatus and Methylosinus trichosporium OB3b and to confirm previous reports that functional expression of protein B and the reductase occurred but the hydroxylase was inactive.
Expanding safe waste management to public health systems
- J. S. Lloyd
- MedicineThe Lancet
- 19 January 2019