William E. Antholine mainly investigates Copper, Crystallography, Biochemistry, Electron paramagnetic resonance and Stereochemistry. His biological study spans a wide range of topics, including Inorganic chemistry, Zinc and Nuclear chemistry. The various areas that he examines in his Crystallography study include Phospholipid, Ground state, Photochemistry, Rotational diffusion and Binding site.
His work in Biochemistry covers topics such as Ribonucleotide reductase which are related to areas like Gallium nitrate and Ligand. William E. Antholine has researched Electron paramagnetic resonance in several fields, including Hyperfine structure, X-ray absorption spectroscopy and Active site. In Stereochemistry, William E. Antholine works on issues like Protein structure, which are connected to Chemical affinity, Sequence and Molecular recognition.
Copper, Electron paramagnetic resonance, Crystallography, Stereochemistry and Biochemistry are his primary areas of study. The Copper study which covers Inorganic chemistry that intersects with Polymer chemistry and Methane monooxygenase. William E. Antholine works mostly in the field of Electron paramagnetic resonance, limiting it down to topics relating to Photochemistry and, in certain cases, Radical, as a part of the same area of interest.
His Crystallography study incorporates themes from Valence and Molecule. His study on Stereochemistry also encompasses disciplines like
His primary scientific interests are in Biochemistry, Electron paramagnetic resonance, Inorganic chemistry, Crystallography and Copper. He has included themes like Chromium, Hyperfine structure, Molecule and Tumor cells in his Electron paramagnetic resonance study. His Chromium research focuses on Hydroxyl radical and how it connects with Hexavalent chromium, Stereochemistry, Plasmid, Cytochrome b5 and DNA damage.
The concepts of his Inorganic chemistry study are interwoven with issues in Methane monooxygenase, Catalysis, Active site and Engineering physics. His studies in Crystallography integrate themes in fields like Paracoccus denitrificans, Amicyanin, Phosphine and Electron transfer. His study in Copper is interdisciplinary in nature, drawing from both Group 2 organometallic chemistry and Ligand.
William E. Antholine mostly deals with Biochemistry, Thioredoxin reductase, Thioredoxin, Reactive oxygen species and Methylococcus capsulatus. The study incorporates disciplines such as Molecular mass, Methylococcaceae, Stereochemistry and Methanobactin in addition to Methylococcus capsulatus. His work carried out in the field of Stereochemistry brings together such families of science as Molecule and Siderophore.
His Methane monooxygenase study integrates concerns from other disciplines, such as Inorganic chemistry, A-site, Trimer and Active site. The Medicinal chemistry study combines topics in areas such as Electron paramagnetic resonance and Catalysis. His Photochemistry research incorporates themes from Copper protein and Copper.
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Molecular Features of the Copper Binding Sites in the Octarepeat Domain of the Prion Protein
Colin S. Burns;Eliah Aronoff-Spencer;Christine M. Dunham;Paula Lario.
Identification of the Cu2+ Binding Sites in the N-Terminal Domain of the Prion Protein by EPR and CD Spectroscopy
Eliah Aronoff-Spencer;Colin S. Burns;Nikolai I. Avdievich;Gary J. Gerfen.
Nature of the Intermediate Formed in the Reduction of O2 to H2O at the Trinuclear Copper Cluster Active Site in Native Laccase
Sang-Kyu Lee;Serena Debeer George;William E. Antholine;Britt Hedman.
Journal of the American Chemical Society (2002)
An EPR Investigation of the Products of the Reaction of Cytosolic and Mitochondrial Aconitases with Nitric Oxide
M. Claire Kennedy;William E. Antholine;Helmut Beinert.
Journal of Biological Chemistry (1997)
Copper coordination in the full-length, recombinant prion protein.
Colin S. Burns;Eliah Aronoff-Spencer;Giuseppe Legname;Stanley B. Prusiner.
Chromium(VI) reductase activity is associated with the cytoplasmic membrane of anaerobically grown Shewanella putrefaciens MR-1.
C. R. Myers;B. P. Carstens;W. E. Antholine;J. M. Myers.
Journal of Applied Microbiology (2001)
The membrane-associated methane monooxygenase (pMMO) and pMMO-NADH:quinone oxidoreductase complex from Methylococcus capsulatus bath
Dong W. Choi;Ryan C. Kunz;Eric S. Boyd;Jeremy D. Semrau.
Journal of Bacteriology (2003)
The octarepeat domain of the prion protein binds Cu(II) with three distinct coordination modes at pH 7.4.
Madhuri Chattopadhyay;Eric D. Walter;Dustin J. Newell;Pilgrim J. Jackson.
Journal of the American Chemical Society (2005)
A comparative EPR investigation of the multicopper proteins nitrous‐oxide reductase and cytochrome c oxidase
William E. Antholine;Dieter H. W. Kastrau;Guy C. M. Steffens;Gerhard Buse.
FEBS Journal (1992)
Synthesis and structural and spectroscopic characterization of mononuclear copper nitrosyl complexes: models for nitric oxide adducts of copper proteins and copper-exchanged zeolites
Christy E. Ruggiero;Susan M. Carrier;William E. Antholine;James W. Whittaker.
Journal of the American Chemical Society (1993)
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