Raven, Emma - University of Leicester - Department of Chemistry

研究领域

Indoleamine 2,3-dioxygenase Substrate Binding and Catalytic Mechanism in Heme Peroxidases Covalent Heme Formation in Peroxidases Experimental Approach Publications

近期论文

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Kwon, H.; Basran, J.; Casadei, C. M.; Fielding, A. J. Schrader, T. E.; Ostermann, A.; Devos, J.; Aller, P.; Blakeley, M. P.; Moody, P. C. E.; Raven, E. L. Direct visualisation of a Fe(IV)-OH intermediate in a heme enzyme. Nature Comm. 2016, 7, Article number: 13445 (doi:10.1038/ncomms13445). Nnamchi, C. I.; Parkin, G.; Efimov, I.; Basran, J.; Kwon, H.; Svistunekno, D. A.; Agirre, J.; Okolo, B. N.; Moneke, A.; Nwanguma, B. C.; Moody, P. C. E.; Raven, E. L. Structural characterisation of a heme peroxidase from Sorghum. J. Biol. Inorg. Chem. 2016, 21, 63-70. Yuan, X.; Rietzschel, N.; Kwon, H.; Da Dilva, A. B. W. N.; Hanna, D.; Phillips, J.; Raven, E. L.; Reddi, A. R.; Hamza, I. Regulation of intracellular heme trafficking revealed by subcellular reporters. Proc. Natl. Acad. Sci. 2016, 113, E5144-5152. Burton, M. J.; Kapetanaki, S. M.; Chernova, T.; Jamieson, A. G.; Dorlet, P.; Santolini, J.; Moody, P. C. E.; Mitcheson, J. S.; Davies, N. W.; Schmid, R.; Raven, E. L.; Storey, N. M. A heme-binding domain controls regulation of ATP-dependent potassium channels. Proc. Natl. Acad. Sci. 2016, 113, 3785. Published as a companion paper (back-to-back) with another heme paper from Prof Saito’s laboratory in Japan. Booth, E. S.; Basran, J.; Lee, M.; Handa, S.; Raven, E. L. Substrate Oxidation by Indoleamine 2,3-Dioxygenase: Evidence for a Common Reaction Mechanism. J. Biol. Chem. 2015, 290, 30924-30930. Casadei, C. M.; Gumiero, A.; Clive L. Metcalfe; Murphy, E. J.; Basran, J.; Concilio, M. G.; Teixeira, S. C. M.; Schrader, T. E.; Fielding, A. J.; Ostermann, A.; Blakeley, M. P.; Raven, E. L.; Moody, P. C. E. Science, 2014, 345, 193-197. ‘Neutron cryo-crystallography captures the protonation state of ferryl heme in a peroxidase.’ This paper was selected for F1000Prime, as being of special significance in its field: F1000Prime link. Jenner, M.; Ellis, J.; Huang, W.-C.; Raven, E. L.; Roberts, G. C. R.; Oldham, N. J. Angew. Chemie. Int Ed, 2011, 50, 8291-8294. ‘Detection of Open and Closed Conformations of NADPH-Cytochrome P450 Reductase by Electrospray Ionisation-Ion Mobility-Mass Spectrometry’. Efimov, I.; Badyal, S. K.; Metcalfe, C. L.; Macdonald, I. K.; Gumiero, A.; Raven, E. L.; Moody, P. C. E. J. Am. Chem. Soc. 2011, 133, 15376-15383. ‘Proton delivery to ferryl heme in a heme peroxidase: enzymatic use of the Grotthuss mechanism.’Basran, J.; Efimov, I.; Chauhan, N.; Thackray, S. J.; Krupa, J.; Eaton, G.; Griffith, G. A.; Mowat, C. G.; Handa, S.; Raven, E. L. J. Am. Chem. Soc. 2011, 133, 16251-16257. ‘The mechanism of formation of N-formylkynurenine by heme deoxygenates.’Murphy, E. J.; Metcalfe, C. L.; Nnamchi, C.; Moody, P. C. E.; Raven, E. L. FEBS Journal, 2012, 279,1632-1639. ‘Crystal structures of guaiacol and phenol bound to a heme peroxidase.’Efimov, I.; Basran, J.; Chauhan, N.; Sun, X.; Chapman, S. K.; Mowat, C. G.; Raven, E. L. J. Am. Chem. Soc. 2012, 134, 3034-3041. ‘The mechanism of substrate inhibition in indoleamine 2,3-dioxygenase.’Chauhan, N.; Basran, J.; Rafice, S.; Efimov, I.; Millett, E. S.; Mowat, C. G.; Moody, P. C. E.; Handa, S.; Raven, E. L. FEBS. J. 2012, 279, 4501-4509. ‘How is the distal pocket of a heme protein optimized for binding of tryptophan?’Huang, W.-C.; Ellis, J. E.; Moody, P. C. E; Raven, E. L.; Roberts, G. C. R. Structure, 2013, 21, 1-9. ‘Redox-linked domain movements in the catalytic cycle of cytochrome P450 reductase.’Efimov, I.; Parkin, G.; Millett, E. S.; Glenday, J.; Chan, C. K.; Weedon, H.; Randhawa, H.; Basran, J. Raven, E. L. FEBS Lett. 2014, 588, 701-704. ‘A simple method for the determination of reduction potentials in heme proteins.’Gumiero, A.; Metcalfe, C. L.; Pearson, A. R.; Raven, E. L.; Moody, P. C. E. J. Biol. Chem. 2011, 286, 1260-1268. ‘The nature of the ferryl heme in Compounds I and II.’ Gumiero, A.; Murphy, E. J.; Metcalfe, C. L.; Moody, P. C. E.; Raven, E. L. Arch. Biochem. Biophys. 2010, 500, 13-20. Special issue of peroxidase chemistry. ‘An analysis of substrate binding interactions in the heme peroxidase enzymes: a structural perspective.’ Davydov, R.; Chauhan, N.; Thackray, S. J.; Anderson, J. L.; Papadopoulou, N.; Mowat, C.; Chapman, S. K.; Raven, E. L.; Hoffman, B. M. J. Amer. Chem. Soc., 2010, 132, 5494-5500. ‘Probing the ternary complexes of indoleamine and tryptophan 2,3-dioxygenases by cryoreduction EPR and ENDOR spectroscopy.’Raven, E. L.; Robinson, N., Nat. Prod. Rep., 2010, 27, 635-636. Metals in cells themed issue. Ortiz de Montellano, P. M.; Raven, E. L., Nat. Prod. Rep. 2007, 24, 499. The chemistry and biochemistry of heme proteins. . Pipirou, Z.; Bottrill, A. R.; Metcalfe, C. M.; Mistry, S. C.; Badyal, S. K.; Rawlings, B. J.; Raven, E. L. Biochemistry 2007, 46, 2174-2180. ‘Autocatalytic Formation of a Covalent Link between Tryptophan 41 and the Heme in Ascorbate Peroxidase.’ Efimov, I.; Papadopoulou, N. D.; McLean, K. J.; Badyal, S. K.; Macdonald, I. K.; Munro, A. W.; Moody, P. C. E.; Raven, E. L. Biochemistry 2007, 46, 8017-8023. ‘The Redox Properties of Ascorbate Peroxidase.’ Metcalfe, C. L.; Daltrop, O.; Ferguson, S. J.; Raven, E. L. Biochem. J. 2007, 408, 355-361. ‘Tuning the formation of a covalent heme-protein link by selection of reductive or oxidative conditions as exemplified by ascorbate peroxidase.’ Pipirou, Z.; Bottrill, A. R.; Svistunenko, D. A.; Efimov, I.; Basran, J.; Mistry, S. C.; Cooper, C. E.; Raven, E. L. Biochemistry 2007, 46, 13269-13278. ’The reactivity of heme in biological systems: autocatalytic formation of both tyrosine-heme and tryptophan-heme covalent links in a single protein architecture.’ Metcalfe, C. L.; Macdonald, I. K.; Murphy, E. J.; Brown, K. A.; Raven, E. L.; Moody, P. C. E. J. Biol. Chem. 2008, J. Biol. Chem. 283, 6193-6200. ‘The tuberculosis prodrug isoniazid bound to activating peroxidases.’ Badyal, S. K.; Metcalfe, C. L.; Basran, J.; Efimov, I.; Moody, P. C. E.; Raven, E. L. Biochemistry 2008, 47, 4403-4409. ‘Iron oxidation state as a molecular trigger controlling active site structure in a heme peroxidase.’