2020 - Fellow of the Royal Society, United Kingdom
The scientist’s investigation covers issues in Stereochemistry, Biochemistry, Cofactor, Flavin group and Enzyme. The Stereochemistry study combines topics in areas such as Biocatalysis, Oxidoreductase, Active site, Flavin mononucleotide and Electron transfer. Nigel S. Scrutton focuses mostly in the field of Active site, narrowing it down to topics relating to Substrate and, in certain cases, Trinitrotoluene and Catalytic cycle.
His Cofactor research integrates issues from Protein structure, Redox, NAD+ kinase and Heme. His Flavin group study also includes
Nigel S. Scrutton spends much of his time researching Stereochemistry, Biochemistry, Enzyme, Photochemistry and Electron transfer. His work deals with themes such as Oxidoreductase, Cofactor, Active site, Substrate and Flavin group, which intersect with Stereochemistry. His Escherichia coli, Mutant, Protein engineering and reductase study in the realm of Biochemistry connects with subjects such as Glutathione reductase.
His primary area of study in Enzyme is in the field of Reductase. Nigel S. Scrutton has researched Photochemistry in several fields, including Reaction rate constant, Hydride, Catalysis and Kinetic isotope effect. His research integrates issues of Electron-transferring flavoprotein, Electron transport chain, Biophysics, Redox and Cytochrome P450 reductase in his study of Electron transfer.
His main research concerns Synthetic biology, Biophysics, Photochemistry, Active site and Computational biology. His studies in Synthetic biology integrate themes in fields like Escherichia coli, Selection, Metabolic engineering and Biochemical engineering. His study focuses on the intersection of Biophysics and fields such as Electron transfer with connections in the field of Redox and Reaction mechanism.
His studies deal with areas such as Spectroscopy, Time-resolved spectroscopy, Flavoprotein and Flavin group as well as Photochemistry. His Active site research is multidisciplinary, relying on both Protochlorophyllide and Stereochemistry. His work focuses on many connections between Stereochemistry and other disciplines, such as Cofactor, that overlap with his field of interest in NAD+ kinase.
His primary areas of study are Synthetic biology, Pipeline, Active site, Computational biology and Biochemical engineering. His work is dedicated to discovering how Synthetic biology, Selection are connected with Multiple sequence alignment and Workflow and other disciplines. Nigel S. Scrutton combines subjects such as Combinatorial chemistry, Stereochemistry, Substrate and Biocatalysis with his study of Active site.
His Stereochemistry study also includes fields such as
Protochlorophyllide most often made with reference to Photosensitizer,
Amino acid which is related to area like Monoterpene. His Biochemical engineering research also works with subjects such as
Speciality chemicals which connect with Metabolic engineering,
Biofuel which is related to area like Biomass. Enzyme is a subfield of Biochemistry that Nigel S. Scrutton explores.
This overview was generated by a machine learning system which analysed the scientist’s body of work. If you have any feedback, you can contact us here.
Redesign of the coenzyme specificity of a dehydrogenase by protein engineering
Nigel S. Scrutton;Alan Berry;Richard N. Perham.
Atomic description of an enzyme reaction dominated by proton tunneling
Laura Masgrau;Anna Roujeinikova;Linus O. Johannissen;Parvinder Hothi.
Cation-pi bonding and amino-aromatic interactions in the biomolecular recognition of substituted ammonium ligands.
Nigel S. Scrutton;Andrew R.C. Raine.
Biochemical Journal (1996)
Enzymatic H-Transfer Requires Vibration-Driven Extreme Tunneling†
Jaswir Basran;Michael J. Sutcliffe;Nigel S. Scrutton.
Biocatalytic Reductions and Chemical Versatility of the Old Yellow Enzyme Family of Flavoprotein Oxidoreductases
Helen S. Toogood;John M. Gardiner;Nigel S. Scrutton.
Conversion of alcohols to enantiopure amines through dual-enzyme hydrogen-borrowing cascades.
Francesco G. Mutti;Tanja Knaus;Nigel S. Scrutton;Michael Breuer.
Good vibrations in enzyme-catalysed reactions
Sam Hay;Nigel S. Scrutton.
Nature Chemistry (2012)
Covalent attachment of flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN) to enzymes: The current state of affairs
Martin Mewies;William S. McIntire;William S. McIntire;William S. McIntire;Nigel S. Scrutton.
Protein Science (1998)
Biotransformation of Explosives by the Old Yellow Enzyme Family of Flavoproteins
Richard E. Williams;Deborah A. Rathbone;Nigel S. Scrutton;Neil C. Bruce.
Applied and Environmental Microbiology (2004)
What's in a covalent bond? On the role and formation of covalently bound flavin cofactors.
Dominic P. H. M. Heuts;Nigel S. Scrutton;William S. McIntire;William S. McIntire;Marco W. Fraaije.
FEBS Journal (2009)
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