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A. Camara-Artigas

Researcher at Arizona State University

Publications -  11
Citations -  417

A. Camara-Artigas is an academic researcher from Arizona State University. The author has contributed to research in topics: Photosynthetic reaction centre & Bacteriochlorophyll. The author has an hindex of 9, co-authored 11 publications receiving 402 citations. Previous affiliations of A. Camara-Artigas include University of Almería.

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Interactions between lipids and bacterial reaction centers determined by protein crystallography.

TL;DR: The structure of the reaction center from Rhodobacter sphaeroides has been solved by using x-ray diffraction at a 2.55-Å resolution limit and three lipid molecules that lie on the surface of the protein are resolved in the electron density maps, suggesting the presence of an “inner shell” of lipids around membrane proteins that is critical for membrane function.
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The structure of the FMO protein from Chlorobium tepidum at 2.2 A resolution.

TL;DR: The bacteriochlorophyll protein, or FMO protein, from Chlorobium tepidum, which serves as a light-harvesting complex and directs light energy from the chlorosomes attached to the cell membrane to the reaction center has been crystallized in a new space group.
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Design of a redox-linked active metal site: manganese bound to bacterial reaction centers at a site resembling that of photosystem II.

TL;DR: In this study, carboxylate residues were introduced by mutagenesis into highly oxidizing reaction centers at a site homologous to the manganese-binding site of photosystem II, illustrating the successful design of a redox active metal center in a protein complex.
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Crystallographic and thermodynamic analysis of the binding of S-octylglutathione to the Tyr 7 to Phe mutant of glutathione S-transferase from Schistosoma japonicum.

TL;DR: The binding of S-octyl-GSH to SjGST(Y7F) is enthalpically and entropically driven at temperatures below 30 degrees C and conformational changes that may be responsible for the lack of binding to the B subunit are observed.
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The structure of the heterodimer reaction center from Rhodobacter sphaeroides at 2.55 å resolution.

TL;DR: Crystals have been obtained of reaction centers of the heterodimer mutant that has significantly different properties than wild type due to the primary donor being formed from both a bacterio chlorophyll and bacteriopheophytin rather than two bacteriochlorophylls as found for wild type.