TAILIEUCHUNG - Báo cáo khoa học: Proton transfer in the oxidative half-reaction of pentaerythritol tetranitrate reductase Structure of the reduced enzyme-progesterone complex and the roles of residues Tyr186, His181 and His184

The roles of His181, His184 and Tyr186 in PETN reductase have been examined by mutagenesis, spectroscopic and stopped-flow kinetics, and by determination of crystallographic structures for the Y186F PETN reductase and reduced wild-type enzyme—progesterone complex. Residues His181 and His184 are important in the binding of coenzyme, steroids, nitro-aromatic ligands and the substrate 2-cyclohexen-1-one. | iFEBS Journal Proton transfer in the oxidative half-reaction of pentaerythritol tetranitrate reductase Structure of the reduced enzyme-progesterone complex and the roles of residues Tyr186 His181 and His184 Huma Khan1 Terez Barna1 Neil C. Bruce2 Andrew W. Munro1 David Leys1 t and Nigel S. Scrutton1 t 1 Department of Biochemistry University of Leicester UK 2 CNAP Department of Biology University of York UK Keywords crystallography flavoprotein mechanism kinetics Old Yellow Enzyme PETN reductase Correspondence N. S. Scrutton Faculty of Life Sciences University of Manchester Stopford Building Oxford Road Manchester M13 9PT UK Fax 44 161 2755586 Tel 44 161 2755632 E-mail Present addresses Manchester Interdisciplinary Biocentre Schoolof ChemicalEngineering and Ana-lyticalScience University of Manchester The Mill PO Box 88 Manchester M60 1QD UK flManchester Interdisciplinary Biocentre and Faculty of Life Sciences Faculty of Life Sciences University of Manchester Stopford Building Oxford Road Manchester M13 9PT UK Received 13 June 2005 revised 15 July 2005 accepted 21 July 2005 doi The roles of His181 His184 and Tyr186 in PETN reductase have been examined by mutagenesis spectroscopic and stopped-flow kinetics and by determination of crystallographic structures for the Y186F PETN reductase and reduced wild-type enzyme progesterone complex. Residues His181 and His184 are important in the binding of coenzyme steroids nitroaromatic ligands and the substrate 2-cyclohexen-1-one. The H181A and H184A enzymes retain activity in reductive and oxidative half-reactions and thus do not play an essential role in catalysis. Ligand binding and catalysis is not substantially impaired in Y186F PETN reductase which contrasts with data for the equivalent mutation Y196F in Old Yellow Enzyme. The structure of Y186F PETN reductase is identical to wild-type enzyme with the obvious exception of the mutation. We show in PETN .

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