Scripps Research Institute
His primary scientific interests are in Stereochemistry, Crystal structure, Crystallography, Aconitase and Protein structure. His work investigates the relationship between Stereochemistry and topics such as Hydrogen bond that intersect with problems in Cubane. His Crystal structure study integrates concerns from other disciplines, such as Metalloprotein and Cysteine.
Much of his study explores Crystallography relationship to DNA nanotechnology. His Aconitase research is multidisciplinary, incorporating perspectives in Substrate and Active site. Many of his studies on Protein structure apply to Iron–sulfur cluster as well.
His primary areas of investigation include Crystallography, Crystal structure, Biochemistry, Stereochemistry and Azotobacter vinelandii. His research in Crystallography intersects with topics in Electron transport chain, Redox and Nucleic acid. His Crystal structure research is multidisciplinary, incorporating elements of Ferricyanide and Iron–sulfur cluster.
His work deals with themes such as Aconitase, Hydrogen bond, Protein structure, Conformational isomerism and NAD+ kinase, which intersect with Stereochemistry. His research integrates issues of Lyase, Substrate and Active site in his study of Aconitase. His studies deal with areas such as Hydrolase and Conformational change as well as Protein structure.
C.D. Stout focuses on Crystallography, Stereochemistry, Protein structure, Active site and Hydride. His Crystallography study combines topics from a wide range of disciplines, such as Ferredoxin and Enzyme. C.D. Stout combines subjects such as Hydrolase, Ionic bonding and Crystal structure with his study of Stereochemistry.
Crystal structure and Aconitase are commonly linked in his work. His Protein structure study incorporates themes from Conformational isomerism and Hydrogen bond. His studies in Hydride integrate themes in fields like Chemical physics and Proton translocation.
The scientist’s investigation covers issues in Protein structure, Stereochemistry, Crystal structure, Crystallography and Hydrolase. He interconnects Lyase, Conformational change, Binding site and Active site in the investigation of issues within Protein structure. C.D. Stout has included themes like Aconitase and Citric acid in his Stereochemistry study.
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ACONITASE AS IRON-SULFUR PROTEIN, ENZYME, AND IRON-REGULATORY PROTEIN
Beinert H;Kennedy Mc;Stout Cd.
Chemical Reviews (1996)
Refined crystal structure of Cd, Zn metallothionein at 2.0 A resolution.
A H Robbins;D E McRee;M Williamson;S A Collett.
Journal of Molecular Biology (1991)
Structures of Human Microsomal Cytochrome P450 2A6 Complexed With Coumarin And Methoxsalen
J.K Yano;M.H Hsu;K.J Griffin;C.D Stout.
Nature Structural & Molecular Biology (2005)
Crystal Structure of Cd,Zn Metallothionein
W. F. Furey;A. H. Robbins;L. L. Clancy;D. R. Winge.
Structure of activated aconitase: formation of the [4Fe-4S] cluster in the crystal.
A H Robbins;C D Stout.
Proceedings of the National Academy of Sciences of the United States of America (1990)
Crystal structures of aconitase with isocitrate and nitroisocitrate bound.
H Lauble;M.C Kennedy;H Beinert;C.D. Stout.
Comparison of the NMR solution structure and the x-ray crystal structure of rat metallothionein-2
Werner Braun;M. Vašák;A. H. Robbins;C. D. Stout.
Proceedings of the National Academy of Sciences of the United States of America (1992)
Structure of mammalian cytochrome P450 2C5 complexed with diclofenac at 2.1 A resolution: evidence for an induced fit model of substrate binding.
M.R Wester;E.F Johnson;C Marques-Soares;S Dijols.
The structure of aconitase
A. H. Robbins;C. D. Stout.
Refinement of the 7 Fe ferredoxin from Azotobacter vinelandii at 1.9 Å resolution
Journal of Molecular Biology (1989)
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