Roger N. F. Thorneley mainly investigates Peroxidase, Horseradish peroxidase, Stereochemistry, Enzyme and Hydrogen peroxide. His Peroxidase research is within the category of Biochemistry. His biological study spans a wide range of topics, including Electron donor and Catalysis.
His work deals with themes such as Phosphoglycerate dehydrogenase, NAD+ kinase, Oxidase test and Mutant, which intersect with Stereochemistry. His Enzyme research integrates issues from Inorganic chemistry, Photochemistry and Lignin. His research integrates issues of Ferric, Wild type, Catalytic cycle, Hexacoordinate and Substrate in his study of Hydrogen peroxide.
His primary areas of study are Nitrogenase, Stereochemistry, Biochemistry, Peroxidase and Photochemistry. Roger N. F. Thorneley has researched Nitrogenase in several fields, including Inorganic chemistry, ATP hydrolysis, Substrate, Electron transfer and Klebsiella pneumoniae. His Stereochemistry research incorporates elements of Chorismate synthase, Catalytic cycle, Mutant and Cofactor.
His Enzyme and Oxidoreductase study, which is part of a larger body of work in Biochemistry, is frequently linked to Photoprotection and Nicotiana sylvestris, bridging the gap between disciplines. His Peroxidase study integrates concerns from other disciplines, such as Ferric, Horseradish peroxidase, Catalysis and Hydrogen peroxide. His Photochemistry study also includes fields such as
His primary scientific interests are in Photochemistry, Biochemistry, Peroxidase, Stereochemistry and Enzyme. Roger N. F. Thorneley focuses mostly in the field of Photochemistry, narrowing it down to matters related to Nitric oxide and, in some cases, Electron donor, Medicinal chemistry and Reaction intermediate. He has included themes like Steady state and Zinc in his Biochemistry study.
His Peroxidase research is multidisciplinary, incorporating elements of Nicotiana tabacum, Phenols, Horseradish peroxidase, Catalysis and Hydrogen peroxide. His Stereochemistry study combines topics in areas such as Phosphoglycerate dehydrogenase, Chorismate synthase and Enzyme activator. His work carried out in the field of Enzyme brings together such families of science as Inorganic chemistry, Oxygen and Infrared spectroscopy.
Roger N. F. Thorneley mostly deals with Biochemistry, Active site, Photochemistry, Inorganic chemistry and Enzyme. His Biochemistry study incorporates themes from Molecular biology and Stereochemistry. His Stereochemistry study combines topics from a wide range of disciplines, such as Phosphoglycerate dehydrogenase, Oxidoreductase and Thiol.
The study incorporates disciplines such as Carbon monoxide, Cubane and Nickel in addition to Photochemistry. In his research, Lignin peroxidase is intimately related to Lignin, which falls under the overarching field of Inorganic chemistry. The various areas that Roger N. F. Thorneley examines in his Enzyme study include Combinatorial chemistry, Hydrogen and Oxygen.
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Expression of a synthetic gene for horseradish peroxidase C in Escherichia coli and folding and activation of the recombinant enzyme with Ca2+ and heme.
A. T. Smith;N. Santama;S. Dacey;M. Edwards.
Journal of Biological Chemistry (1990)
Mechanism of Reaction of Hydrogen Peroxide with Horseradish Peroxidase: Identification of Intermediates in the Catalytic Cycle
Jose Neptuno Rodriguez-Lopez;David J. Lowe;Josefa Hernandez-Ruiz;Alexander N. P. Hiner.
Journal of the American Chemical Society (2001)
Phenol-oxidizing peroxidases contribute to the protection of plants from ultraviolet radiation stress
Marcel A.K. Jansen;Ria E. van den Noort;M.Y. Adillah Tan;Els Prinsen.
Plant Physiology (2001)
Role of Arginine 38 in Horseradish Peroxidase A CRITICAL RESIDUE FOR SUBSTRATE BINDING AND CATALYSIS
Jose Neptuno Rodriguez-Lopez;Andrew T. Smith;Roger N.F. Thorneley.
Journal of Biological Chemistry (1996)
A convenient electrochemical preparation of reduced methyl viologen and a kinetic study of the reaction with oxygen using an anaerobic stopped-flow apparatus.
Roger N.F. Thorneley.
Biochimica et Biophysica Acta (1974)
Mechanisms of compound I formation in heme peroxidases.
Alexander N.P. Hiner;Emma L. Raven;Roger N.F. Thorneley;Francisco Garcı́a-Cánovas.
Journal of Inorganic Biochemistry (2002)
Zinc Is a Potent Inhibitor of Thiol Oxidoreductase Activity and Stimulates Reactive Oxygen Species Production by Lipoamide Dehydrogenase
Irina G. Gazaryan;Boris F. Krasnikov;Gillian A. Ashby;Roger N.F. Thorneley.
Journal of Biological Chemistry (2002)
Mechanism of indole-3-acetic acid oxidation by plant peroxidases: anaerobic stopped-flow spectrophotometric studies on horseradish and tobacco peroxidases
I. G. Gazaryan;L. M. Lagrimini;G. A. Ashby;R. N. F. Thorneley.
Biochemical Journal (1996)
The antifolate activity of tea catechins.
Enma Navarro-Perán;Juan Cabezas-Herrera;Francisco García-Cánovas;Marcus C. Durrant.
Cancer Research (2005)
Direct electron transfer between ligninolytic redox enzymes and electrodes
Andreas Christenson;Nina Dimcheva;Elena E. Ferapontova;Lo Gorton.
Electroanalysis (2004)
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