His main research concerns Biochemistry, Stereochemistry, Cytochrome P450, Heme and Active site. His study in Stereochemistry is interdisciplinary in nature, drawing from both Redox, Bacillus megaterium, Substrate and Binding site. His Cytochrome P450 research incorporates elements of Protein structure, Sterol and Mycobacterium tuberculosis.
His Heme research is multidisciplinary, incorporating elements of Nitric oxide synthase, Oxidative phosphorylation, Mutant, Cofactor and Electron transfer. His Active site research incorporates themes from Amino acid and Fatty acid. His Enzyme research is multidisciplinary, relying on both SUPERFAMILY and Biocatalysis.
Andrew W. Munro mostly deals with Stereochemistry, Biochemistry, Cytochrome P450, Heme and Enzyme. Andrew W. Munro interconnects Oxidoreductase, Cofactor, Active site, Substrate and Flavin group in the investigation of issues within Stereochemistry. The Flavin group study combines topics in areas such as Photochemistry, Electron transfer, Flavoprotein and Semiquinone.
His Biochemistry study incorporates themes from Redox and Bacillus megaterium. His Cytochrome P450 research integrates issues from Protein structure, Hydroxylation, Drug metabolism and Mycobacterium tuberculosis. The study incorporates disciplines such as Ferric, Resonance Raman spectroscopy, Crystallography and Ligand in addition to Heme.
Andrew W. Munro mainly focuses on Stereochemistry, Heme, Cytochrome P450, Enzyme and Mycobacterium tuberculosis. Andrew W. Munro has included themes like Oxidoreductase, Crystal structure, Substrate and Active site in his Stereochemistry study. His work in the fields of Heme, such as Heme oxygenase, overlaps with other areas such as Azole.
His Cytochrome P450 study introduces a deeper knowledge of Biochemistry. His Enzyme research is multidisciplinary, incorporating perspectives in Directed evolution, Decarboxylation, Pathogenicity and Tuberculosis. The various areas that he examines in his Mycobacterium tuberculosis study include Structural homology, Enzyme structure, Molecular model, Gene and Drug discovery.
His scientific interests lie mostly in Stereochemistry, Biochemistry, Enzyme, Hydroxylation and Heme. Andrew W. Munro has researched Stereochemistry in several fields, including Substrate, Binding site and Active site. In general Biochemistry, his work in Cytochrome P450, Penicillium chrysogenum and Pravastatin is often linked to Amycolatopsis orientalis linking many areas of study.
His research in Cytochrome P450 focuses on subjects like Oxidative phosphorylation, which are connected to NAD+ kinase, Cytochrome P450 reductase, Ferredoxin, Redox and Coenzyme Q – cytochrome c reductase. His study in Hydroxylation is interdisciplinary in nature, drawing from both Regioselectivity, Rational design, Saturated mutagenesis, Enzyme structure and Stereoselectivity. His biological study spans a wide range of topics, including Protein structure, Decarboxylation, Dissociation and Tetramer.
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P450 BM3: the very model of a modern flavocytochrome.
Andrew W Munro;David G Leys;Kirsty J McLean;Ker R Marshall.
Trends in Biochemical Sciences (2002)
Roles of key active-site residues in flavocytochrome P450 BM3
Michael A. Noble;Caroline S. Miles;Stephen K. Chapman;Dominikus A. Lysek.
Biochemical Journal (1999)
Unusual Cytochrome P450 Enzymes and Reactions
F. Peter Guengerich;Andrew W. Munro.
Journal of Biological Chemistry (2013)
Variations on a (t)heme--novel mechanisms, redox partners and catalytic functions in the cytochrome P450 superfamily.
Andrew W. Munro;Hazel M. Girvan;Kirsty J. McLean.
Natural Product Reports (2007)
Redox Control of the Catalytic Cycle of Flavocytochrome P-450 BM3†
S N Daff;Stephen K Chapman;K L Turner;R A Holt.
Biochemistry (1997)
Cytochrome P450--redox partner fusion enzymes.
Andrew W. Munro;Hazel M. Girvan;Kirsty J. McLean.
Biochimica et Biophysica Acta (2007)
Rapid Rule-out of Acute Myocardial Infarction With a Single High-Sensitivity Cardiac Troponin T Measurement Below the Limit of Detection: A Collaborative Meta-analysis
John W Pickering;Martin P Than;Louise Cullen;Sally Aldous.
Annals of Internal Medicine (2017)
What makes a P450 tick
Andrew W. Munro;Hazel M. Girvan;Amy E. Mason;Adrian J. Dunford.
Trends in Biochemical Sciences (2013)
Applications of microbial cytochrome P450 enzymes in biotechnology and synthetic biology
Hazel M Girvan;Andrew W Munro.
Current Opinion in Chemical Biology (2016)
Azole antifungals are potent inhibitors of cytochrome P450 mono-oxygenases and bacterial growth in mycobacteria and streptomycetes
Kirsty J. McLean;Ker R. Marshall;Alison Richmond;Iain S. Hunter.
Microbiology (2002)
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