Stephen G. Bell

Affiliations: 
2010 Chemistry University of Oxford, Oxford, United Kingdom 
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"Stephen Bell"
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Podgorski MN, Harbort JS, Coleman T, et al. (2020) Biophysical techniques to distinguish ligand binding modes in cytochrome P450 monooxygenases. Biochemistry
Bowen AM, Johnson EOD, Mercuri F, et al. (2017) A Structural Model of a P450-Ferredoxin Complex from Orientation-Selective Double Electron-Electron Resonance Spectroscopy. Journal of the American Chemical Society
Stok JE, Hall EA, Stone ISJ, et al. (2016) In vivo and in vitro hydroxylation of cineole and camphor by cytochromes P450CYP101A1, CYP101B1 and N242A CYP176A1 Journal of Molecular Catalysis B: Enzymatic. 128: 52-64
Munday SD, Shoji O, Watanabe Y, et al. (2015) Improved oxidation of aromatic and aliphatic hydrocarbons using rate enhancing variants of P450Bm3 in combination with decoy molecules. Chemical Communications (Cambridge, England)
Liang K, Coghlan CJ, Bell SG, et al. (2015) Enzyme encapsulation in zeolitic imidazolate frameworks: a comparison between controlled co-precipitation and biomimetic mineralisation. Chemical Communications (Cambridge, England)
Liang K, Ricco R, Doherty CM, et al. (2015) Biomimetic mineralization of metal-organic frameworks as protective coatings for biomacromolecules. Nature Communications. 6: 7240
Zhang A, Zhang T, Hall EA, et al. (2015) The crystal structure of the versatile cytochrome P450 enzyme CYP109B1 from Bacillus subtilis. Molecular Biosystems. 11: 869-81
Coleman T, Chao RR, Bruning JB, et al. (2015) CYP199A4 catalyses the efficient demethylation and demethenylation of para-substituted benzoic acid derivatives Rsc Advances. 5: 52007-52018
Hall EA, Bell SG. (2015) The efficient and selective biocatalytic oxidation of norisoprenoid and aromatic substrates by CYP101B1 from Novosphingobium aromaticivorans DSM12444 Rsc Advances. 5: 5762-5773
Zhang T, Zhang A, Bell SG, et al. (2014) The structure of a novel electron-transfer ferredoxin from Rhodopseudomonas palustris HaA2 which contains a histidine residue in its iron-sulfur cluster-binding motif. Acta Crystallographica. Section D, Biological Crystallography. 70: 1453-64
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