Myles R. Cheesman
Centre for Metalloprotein Spectroscopy and Biology
School of Chemical Sciences
University of East Anglia
Norwich NR4 7TJ
U.K
Name/email consistency: high
- The nature of the exchange coupling between high-spin Fe(III) heme o3 and CuBII in Escherichia coli quinol oxidase, cytochrome bo3: MCD and EPR studies. Cheesman, M.R., Oganesyan, V.S., Watmough, N.J., Butler, C.S., Thomson, A.J. J. Am. Chem. Soc. (2004)
- Novel heme ligation in a c-type cytochrome involved in thiosulfate oxidation: EPR and MCD of SoxAX from Rhodovulum sulfidophilum. Cheesman, M.R., Little, P.J., Berks, B.C. Biochemistry (2001)
- The MCD and EPR of the heme centers of nitric oxide reductase from Pseudomonas stutzeri: evidence that the enzyme is structurally related to the heme-copper oxidases. Cheesman, M.R., Zumft, W.G., Thomson, A.J. Biochemistry (1998)
- Two enzymes with a common function but different heme ligands in the forms as isolated. Optical and magnetic properties of the heme groups in the oxidized forms of nitrite reductase, cytochrome cd1, from Pseudomonas stutzeri and Thiosphaera pantotropha. Cheesman, M.R., Ferguson, S.J., Moir, J.W., Richardson, D.J., Zumft, W.G., Thomson, A.J. Biochemistry (1997)
