2007 - Fellow of the American Association for the Advancement of Science (AAAS)
John D. Lipscomb spends much of his time researching Stereochemistry, Methane monooxygenase, Substrate, Active site and Dioxygenase. The various areas that John D. Lipscomb examines in his Stereochemistry study include Oxidoreductase, Enzyme, Hydroxylation, Electron paramagnetic resonance and Binding site. His Methane monooxygenase research includes themes of Reaction intermediate, Photochemistry, Catalytic cycle and Reductase.
His Substrate study introduces a deeper knowledge of Biochemistry. His research integrates issues of Ligand and Crystal structure in his study of Active site. As a part of the same scientific family, John D. Lipscomb mostly works in the field of Dioxygenase, focusing on Cleavage and, on occasion, Enzyme inhibitor, Molecular mass and Oligomer.
John D. Lipscomb mainly focuses on Stereochemistry, Methane monooxygenase, Active site, Dioxygenase and Substrate. His study in Stereochemistry is interdisciplinary in nature, drawing from both Oxygenase, Enzyme, Electron paramagnetic resonance, Catalysis and Binding site. His studies in Methane monooxygenase integrate themes in fields like Photochemistry and Catalytic cycle.
The Active site study which covers Crystallography that intersects with Ferric, Inorganic chemistry and Cytochrome. His Catechol dioxygenase study in the realm of Dioxygenase interacts with subjects such as Ligand. His research in Substrate intersects with topics in Bond cleavage, Metal and Hydroxylation.
Stereochemistry, Active site, Catalysis, Methane monooxygenase and Photochemistry are his primary areas of study. The various areas that he examines in his Stereochemistry study include Oxygenase, Nonribosomal peptide, Biosynthesis, Oxidoreductase and Dioxygenase. The study incorporates disciplines such as Crystal structure, Catalytic cycle, Substrate, Density functional theory and Histidine in addition to Active site.
His Catalysis study incorporates themes from Oxidizing agent, Molecule, Redox and Chromophore. He interconnects Nonanal, Heptanal and X-ray absorption spectroscopy, Absorption spectroscopy in the investigation of issues within Methane monooxygenase. The Photochemistry study combines topics in areas such as Mössbauer spectroscopy, Bond cleavage, Reactive intermediate and Semiquinone.
John D. Lipscomb mainly investigates Methane monooxygenase, Stereochemistry, Methane, Oxygenase and Photochemistry. His Methane monooxygenase study is associated with Organic chemistry. His Stereochemistry research is multidisciplinary, incorporating elements of Biochemistry, Catalysis, Active site, Electron paramagnetic resonance and Metal.
He has researched Catalysis in several fields, including Combinatorial chemistry, Catechol, Substrate and Binding site. His Active site research includes elements of Single crystal, Moiety, Crystal structure, Catalytic cycle and Aromatic amine. His Photochemistry study integrates concerns from other disciplines, such as Scientific method, Monooxygenase, Methanol, Molecule and Oxygen.
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Dioxygen activation by enzymes containing binuclear non-heme iron clusters
Bradley J. Wallar;John D. Lipscomb.
Chemical Reviews (1996)
An Fe2IVO2 Diamond Core Structure for the Key Intermediate Q of Methane Monooxygenase
Lijin Shu;Jeremy C. Nesheim;Karl Kauffmann;Eckard Münck.
Versatility of biological non-heme Fe(II) centers in oxygen activation reactions
Elena G Kovaleva;John D Lipscomb.
Nature Chemical Biology (2008)
Haloalkene oxidation by the soluble methane monooxygenase from Methylosinus trichosporium OB3b: Mechanistic and environmental implications
Brian G. Fox;James G. Borneman;Lawrence P. Wackett;John D. Lipscomb.
Biochemistry of the Soluble Methane Monooxygenase
John D. Lipscomb.
Annual Review of Microbiology (1994)
Methane monooxygenase from Methylosinus trichosporium OB3b. Purification and properties of a three-component system with high specific activity from a type II methanotroph.
B. G. Fox;W. A. Froland;J. E. Dege;John D Lipscomb.
Journal of Biological Chemistry (1989)
Transient intermediates of the methane monooxygenase catalytic cycle.
Sang Kyu Lee;Jeremy C. Nesheim;John D Lipscomb.
Journal of Biological Chemistry (1993)
A Transient Intermediate of the Methane Monooxygenase Catalytic Cycle Containing an FeIVFeIV Cluster
Sang Kyu Lee;Brian G. Fox;Wayne A. Froland;John D. Lipscomb.
Journal of the American Chemical Society (1993)
Crystal structures of Fe2+ dioxygenase superoxo, alkylperoxo, and bound product intermediates.
Elena G. Kovaleva;John D. Lipscomb.
Crystal structure of the hydroxylase component of methane monooxygenase from Methylosinus trichosporium OB3b.
Nates An Elango;Ramaswamy Radhakrishnan;Wayne A. Froland;Bradley J. Wallar.
Protein Science (1997)
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