Ninian J. Blackburn focuses on Copper, Crystallography, Ligand, Metal and Stereochemistry. His Copper research includes elements of Inorganic chemistry, Extended X-ray absorption fine structure and Histidine. The various areas that Ninian J. Blackburn examines in his Crystallography study include Cysteine, Protein structure, Azurin, Binding site and Absorption spectroscopy.
His research in Ligand tackles topics such as Electron transfer which are related to areas like Coordination number, Oxidation state, Transition metal, Steric effects and Stoichiometry. While the research belongs to areas of Metal, Ninian J. Blackburn spends his time largely on the problem of Periplasmic space, intersecting his research to questions surrounding Isothermal titration calorimetry and Transport protein. His Stereochemistry research is multidisciplinary, relying on both Bifunctional, Active site, Enzyme and Photochemistry.
His primary scientific interests are in Copper, Stereochemistry, Crystallography, Ligand and Inorganic chemistry. His Copper research incorporates elements of Photochemistry, Reactivity, Metal and Extended X-ray absorption fine structure. The study incorporates disciplines such as Active site, Enzyme, Hydroxylation and Electron transfer in addition to Stereochemistry.
His Crystallography study incorporates themes from X-ray absorption spectroscopy, Absorption spectroscopy, Cysteine and Binding site. His work in Ligand is not limited to one particular discipline; it also encompasses Histidine. Ninian J. Blackburn has included themes like Carbon monoxide and Molecule in his Inorganic chemistry study.
His scientific interests lie mostly in Copper, Stereochemistry, Crystallography, Electron transfer and Peptidylglycine monooxygenase. His biological study spans a wide range of topics, including Metalloprotein, Metal, Periplasmic space, Inorganic chemistry and Biochemistry. His study in Inorganic chemistry is interdisciplinary in nature, drawing from both Tripeptide, Adduct and Dimer.
His Stereochemistry study combines topics from a wide range of disciplines, such as Active site, Ligand and Hydroxylation. His Crystallography research includes themes of Molecule, Cysteine, Cofactor and Copper protein. His study explores the link between Electron transfer and topics such as Thermus thermophilus that cross with problems in Proton-coupled electron transfer and Azurina.
The scientist’s investigation covers issues in Copper, Crystallography, Periplasmic space, Efflux and Stereochemistry. The concepts of his Copper study are interwoven with issues in ATP7A, ATPase and Photochemistry. His research in Crystallography intersects with topics in Molecule, Cytochrome c oxidase, Electron Transport Complex IV and Copper protein.
His Efflux study also includes
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Three-dimensional structure of the human copper transporter hCTR1
Christopher J. De Feo;Stephen G. Aller;Stephen G. Aller;Gnana S. Siluvai;Ninian J. Blackburn.
Proceedings of the National Academy of Sciences of the United States of America (2009)
Metal-metal bonding in biology: EXAFS evidence for a 2.5 A copper-copper bond in the CuA center of cytochrome oxidase.
Ninian J. Blackburn;Mary E. Barr;William H. Woodruff;John van der Ooost.
Dioxygen−copper reactivity: generation, characterization, and reactivity of a hydroperoxo−dicopper(II) complex
Kenneth D. Karlin;Phalguni. Ghosh;Richard W. Cruse;Amjad. Farooq.
Journal of the American Chemical Society (1988)
Structural Studies of Copper(I) Complexes of Amyloid‐β Peptide Fragments: Formation of Two‐Coordinate Bis(histidine) Complexes
Richard A. Himes;Ga Young Park;Gnana Sutha Siluvai;Ninian J. Blackburn.
Angewandte Chemie (2008)
Direct metal transfer between periplasmic proteins identifies a bacterial copper chaperone.
Ireena Bagai;Christopher Rensing;Ninian J. Blackburn;Megan M. McEvoy.
Hydrogen Tunneling in Peptidylglycine α-Hydroxylating Monooxygenase
Wilson A. Francisco;Michael J. Knapp;Ninian J. Blackburn;Judith P. Klinman.
Journal of the American Chemical Society (2002)
The CuA domain of Thermus thermophilus ba3-type cytochrome c oxidase at 1.6 A resolution.
Pamela A. Williams;Ninian J. Blackburn;Donita Sanders;Donita Sanders;Henry Bellamy.
Nature Structural & Molecular Biology (1999)
Unusual Cu(I)/Ag(I) coordination of Escherichia coli CusF as revealed by atomic resolution crystallography and X‐ray absorption spectroscopy
Isabell R. Loftin;Sylvia Franke;Sylvia Franke;Ninian J. Blackburn;Megan M. McEvoy.
Protein Science (2007)
An extended-X-ray-absorption-fine-structure study of bovine erythrocyte superoxide dismutase in aqueous solution. Direct evidence for three-co-ordinate Cu(I) in reduced enzyme.
N J Blackburn;S S Hasnain;N Binsted;G P Diakun.
Biochemical Journal (1984)
Substrate-linked Conformational Change in the Periplasmic Component of a Cu(I)/Ag(I) Efflux System
Ireena Bagai;Wenbo Liu;Christopher Rensing;Ninian J. Blackburn.
Journal of Biological Chemistry (2007)
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