His main research concerns Active site, Hydrogenase, Crystallography, Protein structure and Stereochemistry. His Active site research integrates issues from Ether and Ethylene glycol. His Hydrogenase research is multidisciplinary, incorporating perspectives in Inorganic chemistry and Photochemistry.
In general Crystallography, his work in Crystal structure and Resolution is often linked to Moorella thermoacetica linking many areas of study. Juan C. Fontecilla-Camps has researched Protein structure in several fields, including Plasma protein binding, Complementarity determining region, Immunology, Molecule and Binding site. His Stereochemistry study combines topics in areas such as Biochemistry, Enzyme, Carboxydothermus hydrogenoformans, Carbon monoxide dehydrogenase and Scorpion Venoms.
His scientific interests lie mostly in Stereochemistry, Crystallography, Active site, Biochemistry and Hydrogenase. Juan C. Fontecilla-Camps combines subjects such as Androctonus australis, Crystal structure, Molecule, Substrate and Protein structure with his study of Stereochemistry. The Protein structure study which covers Binding site that intersects with Peptide sequence.
His study in the fields of Resolution and Crystal under the domain of Crystallography overlaps with other disciplines such as Micelle. His Active site research includes themes of Carbon monoxide dehydrogenase and Nickel. His Hydrogenase research incorporates themes from Sulfur, Inorganic chemistry, Redox, Ligand and Photochemistry.
His primary areas of study are Stereochemistry, Active site, Cofactor, Tryptophan and Biochemistry. The various areas that Juan C. Fontecilla-Camps examines in his Stereochemistry study include Tyrosine, Lyase, Metal, Substrate and Protein structure. As a part of the same scientific study, he usually deals with the Protein structure, concentrating on Mutagenesis and frequently concerns with Crystal structure and Hydrogenase.
Hydrogenase is closely attributed to Redox in his study. Juan C. Fontecilla-Camps connects Active site with Electron paramagnetic resonance in his study. His work is dedicated to discovering how Mutant, Hydrogen bond are connected with Enzyme and other disciplines.
Juan C. Fontecilla-Camps spends much of his time researching Ligand, Stereochemistry, Lyase, Tryptophan and Peroxide. His study in Ligand is interdisciplinary in nature, drawing from both Formate, Moiety, Medicinal chemistry and Rhodium. He performs multidisciplinary study in Stereochemistry and Nosiheptide in his work.
His Lyase study combines topics from a wide range of disciplines, such as Hydrogen bond, Mutant and Aromatic amino acids. His Peroxide research integrates issues from Fourier transform infrared spectroscopy, Crystallography, Hydroxide and Sulfenic acid. His work deals with themes such as Tyrosine, Active site, Indole test, Photochemistry and Substrate, which intersect with Radical.
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Desulfovibrio desulfuricans iron hydrogenase: the structure shows unusual coordination to an active site Fe binuclear center.
Yvain Nicolet;Claudine Piras;Pierre Legrand;Claude E Hatchikian.
Structure (1999)
Crystal structure of human butyrylcholinesterase and of its complexes with substrate and products.
Yvain Nicolet;Oksana Lockridge;Patrick Masson;Juan C. Fontecilla-Camps.
Journal of Biological Chemistry (2003)
A novel FeS cluster in Fe-only hydrogenases.
Yvain Nicolet;Brian J Lemon;Juan C Fontecilla-Camps;John W Peters.
Trends in Biochemical Sciences (2000)
Ni-Zn-[Fe4-S4] and Ni-Ni-[Fe4-S4] clusters in closed and open subunits of acetyl-CoA synthase/carbon monoxide dehydrogenase.
Claudine Darnault;Anne Volbeda;Eun Jin Kim;Pierre Legrand.
Nature Structural & Molecular Biology (2003)
Gas access to the active site of Ni-Fe hydrogenases probed by X-ray crystallography and molecular dynamics.
Yaël Montet;Patricia Amara;Anne Volbeda;Xavier Vernede.
Nature Structural & Molecular Biology (1997)
The Crystal Structure of the Globular Head of Complement Protein C1q Provides a Basis for Its Versatile Recognition Properties
Christine Gaboriaud;Jordi Juanhuix;Arnaud Gruez;Monique Lacroix.
Journal of Biological Chemistry (2003)
Structural differences between the ready and unready oxidized states of [NiFe] hydrogenases
Anne Volbeda;Lydie Martin;Christine Cavazza;Michaël Matho.
Journal of Biological Inorganic Chemistry (2005)
Crystal structure of a T cell receptor bound to an allogeneic MHC molecule
Jean-Baptiste Reiser;Claudine Darnault;Annick Guimezanes;Claude Grégoire.
Nature Immunology (2000)
A T Cell Receptor CDR3β Loop Undergoes Conformational Changes of Unprecedented Magnitude Upon Binding to a Peptide/MHC Class I Complex
Jean Baptiste Reiser;Claude Grégoire;Claudine Darnault;Thomas Mosser.
Immunity (2002)
The structure of a complex of human 17β-hydroxysteroid dehydrogenase with estradiol and NADP+ identifies two principal targets for the design of inhibitors
Rock Breton;Dominique Housset;Catherine Mazza;Juan Carlos Fontecilla-Camps.
Structure (1996)
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