Architecture of the Photosynthetic Oxygen-Evolving Center

Science

Volumn 303, Issue 5665, 2004, Pages 1831-1838

  Ferreira, Kristina N ^a   Iverson, Tina M ^a   Maghlaoui, Karim ^a   Barber, James ^a   Iwata, So ^a,b  

^a IMPERIAL COLLEGE LONDON   (United Kingdom)

^b JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BACTERIA; CATALYSIS; COORDINATION REACTIONS; DIMERS; OXIDATION; OXYGEN; WATER;

OXYGEN-EVOLVING CENTER (OEC); PHOTOSYSTEMS;

PHOTOSYNTHESIS;

AMINO ACID; BACTERIOCHLOROPHYLL; BETA CAROTENE; CARBON; CARBON DIOXIDE; CAROTENOID; CYTOCHROME; DIMER; IRON; MANGANESE; MONOMER; OXYGEN; PLASTOQUINONE;

PHOTOSYNTHESIS;

AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; CATALYSIS; CRYSTAL STRUCTURE; CYANOBACTERIUM; ELECTRON TRANSPORT; NONHUMAN; OXIDATION; PHOTOSYNTHESIS; PHOTOSYSTEM II; PRIORITY JOURNAL;

BETA CAROTENE; BINDING SITES; CALCIUM; CAROTENOIDS; CHLOROPHYLL; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; CYANOBACTERIA; DIMERIZATION; ELECTRON TRANSPORT; FREE RADICALS; HISTIDINE; HYDROGEN BONDING; LIGANDS; MANGANESE; MODELS, CHEMICAL; MODELS, MOLECULAR; OXIDATION-REDUCTION; OXYGEN; PHOTOSYNTHETIC REACTION CENTER COMPLEX PROTEINS; PHOTOSYSTEM II PROTEIN COMPLEX; PROTEIN CONFORMATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS; TYROSINE; WATER;

BACTERIA (MICROORGANISMS); THERMOSYNECHOCOCCUS ELONGATUS;

EID: 1642331709     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.1093087     Document Type: Article

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52. The authors dedicate this paper to G. T. Babcock and M. P. Klein, J.B. and S.I. acknowledge support from the Biotechnology and Biological Research Science Council. We thank the Centre for Structural Biology and Bioinformatics Facility at Imperial College London for technical support; and C. Schulze-Briese and T. Tomizaki at PX06SA/SLS, Paul Scherrer Institute, Villigen, Switzerland; B. Shepard at ID29; and M. Iwata of the ERATO ATP System Project for help with data collections. T.M.I. has been a Life Sciences Research Foundation Fellow of the Howard Hughes Medical Institute, a European Molecular Biology Organization Long-Term Fellow, and a Ruth L. Kirschstein National Research Science Award Fellow and acknowledges support from D. C. Rees during the initial stages of the study. We wish to thank P. Siegbahn, M. Lundberg, P. Nixon, C. Dismukes, and A. Telfer for comments and helpful discussions. The coordinates, together with the structure factors native, Mn-edge and long wavelength (2.25 Å, for Ca detection), and the experimental multi-wavelength anomalous dispersion (MAD) phases have been deposited in the Protein Data Bank (entry 1S5L) and will be available upon publication.