2006 - Fellow of the American Association for the Advancement of Science (AAAS)
Stereochemistry, Flavin group, Substrate, Photochemistry and Flavoprotein are his primary areas of study. David P. Ballou combines subjects such as Reductase, Cofactor, Steady state, Cytochrome and Hemeprotein with his study of Stereochemistry. His Flavin group research entails a greater understanding of Enzyme.
His biological study spans a wide range of topics, including Active site, Dephosphorylation and Hydroxylation. In Photochemistry, David P. Ballou works on issues like Xanthine oxidase, which are connected to Superoxide dismutase. His work investigates the relationship between Flavoprotein and topics such as Redox that intersect with problems in Flavin reductase.
His primary areas of study are Stereochemistry, Flavin group, Biochemistry, Enzyme and Flavoprotein. His Stereochemistry research is multidisciplinary, relying on both Reductase, Hydroxylation, Cofactor, Active site and Substrate. The concepts of his Flavin group study are interwoven with issues in Mutant, Photochemistry, Flavin adenine dinucleotide and Oxygen.
His Cytochrome, Microsome, Thioredoxin and Tryptophan study in the realm of Biochemistry connects with subjects such as Glutathione reductase. His studies in Enzyme integrate themes in fields like Reactivity and Escherichia coli. The Flavoprotein study combines topics in areas such as Oxidoreductase, Oxidative phosphorylation, Monooxygenase and Redox.
His scientific interests lie mostly in Biochemistry, Flavin group, Stereochemistry, Flavoprotein and Monooxygenase. He has included themes like Photochemistry, Reductase and Substrate in his Flavin group study. His studies deal with areas such as Residue, Liberation and Catalysis, Aldehyde as well as Photochemistry.
His Stereochemistry research includes elements of Hydroxylation, Cofactor, Peroxidase, Reaction rate constant and Steady state. His study in Flavoprotein is interdisciplinary in nature, drawing from both Flavin adenine dinucleotide, Sulfur, Inorganic chemistry, Sulfite and Sulfide. In his research, Oxidoreductase is intimately related to Flavin mononucleotide, which falls under the overarching field of Monooxygenase.
David P. Ballou mostly deals with Biochemistry, Flavin group, Stereochemistry, Flavoprotein and Glutaredoxin. His work on Hydroxylation and Mutagenesis as part of general Biochemistry study is frequently connected to CYP2B6, therefore bridging the gap between diverse disciplines of science and establishing a new relationship between them. His Flavin group research incorporates themes from Flavin adenine dinucleotide and Monooxygenase, Mixed Function Oxygenases.
His research in the fields of Circular dichroism overlaps with other disciplines such as Magnetic circular dichroism. As a part of the same scientific study, David P. Ballou usually deals with the Flavoprotein, concentrating on Sulfide and frequently concerns with Combinatorial chemistry, Catalytic cycle, Photochemistry and Thiosulfate. His Glutaredoxin research is multidisciplinary, incorporating elements of Protein disulfide-isomerase, Protein Data Bank and Active site.
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Flavin-oxygen derivatives involved in hydroxylation by p-hydroxybenzoate hydroxylase.
B Entsch;D P Ballou;V Massey.
Journal of Biological Chemistry (1976)
Oxidative Protein Folding Is Driven by the Electron Transport System
Martin Bader;Wilson Muse;David P Ballou;Christian Gassner.
A molecular basis for nitric oxide sensing by soluble guanylate cyclase
Yunde Zhao;Philip E. Brandish;David P. Ballou;Michael A. Marletta.
Proceedings of the National Academy of Sciences of the United States of America (1999)
The Mechanism of Action of Xanthine Oxidase
John S. Olson;David P. Ballou;Graham Palmer;Vincent Massey.
Journal of Biological Chemistry (1974)
Separate roles for FMN and FAD in catalysis by liver microsomal NADPH-cytochrome P-450 reductase.
J L Vermilion;D P Ballou;V Massey;M J Coon.
Journal of Biological Chemistry (1981)
Phthalate Dioxygenase Reductase: A Modular Structure for Electron Transfer from Pyridine Nucleotides to [2Fe-2S]
Carl C. Correll;Christopher J. Batie;Christopher J. Batie;David P. Ballou;Martha L. Ludwig.
Direct demonstration of superoxide anion production during the oxidation of reduced flavin and of its catalytic decomposition by erythrocuprein.
David Ballou;Graham Palmer;Vincent Massey.
Biochemical and Biophysical Research Communications (1969)
Reactivity of small thiolate anions and cysteine-25 in papain toward methyl methanethiosulfonate.
David D. Roberts;Sidney D. Lewis;David P. Ballou;Steven T. Olson.
Electron−nuclear double resonance spectroscopy of 15N-enriched phthalate dioxygenase from Pseudomonas cepacia proves that two histidines are coordinated to the [2Fe-2S] Rieske-type clusters
Ryszard J. Gurbiel;Christopher J. Batie;Mohanram Sivaraja;Anne E. True.
Mechanistic studies on cyclohexanone oxygenase
Carol Cummings Ryerson;David P. Ballou;Christopher Walsh.
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