title: Gating mechanisms for biological electron transfer: integrating structure with biophysics reveals the nature of redox control in cytochrome P450 reductase and copper-dependent nitrite reductase.
abstract: Biological electron transfer is a fundamentally important reaction. Despite the apparent simplicity of these reactions (in that no bonds are made or broken), their experimental interrogation is often complicated because of adiabatic control exerted through associated chemical and conformational change. We have studied the nature of this control in several enzyme systems, cytochrome P450 reductase, methionine synthase reductase and copper-dependent nitrite reductase. Specifically, we review the evidence for conformational control in cytochrome P450 reductase and methionine synthase reductase and chemical control i.e. proton coupled electron transfer in nitrite reductase. This evidence has accrued through the use and integration of structural, spectroscopic and advanced kinetic methods. This integrated approach is shown to be powerful in dissecting control mechanisms for biological electron transfer and will likely find widespread application in the study of related biological redox systems.
authors.affiliation: Manchester Interdisciplinary Biocentre, Faculty of Life Sciences, University of Manchester, 131 Princess Street, Manchester M1 7DN, United Kingdom.
authors.forename: Nicole G H
authors.initials: NG
authors.lastname: Leferink
authors.forename: Christopher R
authors.initials: CR
authors.lastname: Pudney
authors.forename: Sibylle
authors.initials: S
authors.lastname: Brenner
authors.forename: Derren J
authors.initials: DJ
authors.lastname: Heyes
authors.forename: Robert R
authors.initials: RR
authors.lastname: Eady
authors.forename: S
authors.initials: S
authors.lastname: Samar Hasnain
authors.forename: Sam
authors.initials: S
authors.lastname: Hay
authors.forename: Stephen E J
authors.initials: SE
authors.lastname: Rigby
authors.forename: Nigel S
authors.initials: NS
authors.lastname: Scrutton
mesh_terms: D042441:Achromobacter denitrificans / Q000201:enzymology; D000818:Animals; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D018360:Crystallography, X-Ray; D004579:Electron Transport; D006801:Humans; D008958:Models, Molecular; D009251:NADPH-Ferrihemoprotein Reductase / Q000737:chemistry* / Q000378:metabolism; D009572:Nitrite Reductases / Q000737:chemistry* / Q000378:metabolism; D010084:Oxidation-Reduction; D011487:Protein Conformation
chemical_list: D001426:Bacterial Proteins; D009251:NADPH-Ferrihemoprotein Reductase; D009572:Nitrite Reductases; C052695:nitrite reductase, copper-containing