Where water is oxidized to dioxygen: Structure of the photosynthetic Mn4Ca cluster

Science

Volumn 314, Issue 5800, 2006, Pages 821-825

  Yano, Junko ^a,b   Kern, Jan ^c   Sauer, Kenneth ^a,b   Latimer, Matthew J ^d   Pushkar, Yulia ^a,b   Biesiadka, Jacek ^e   Loll, Bernhard ^e,g   Saenger, Wolfram ^e   Messinger, Johannes ^f   Zouni, Athina ^c   Yachandra, Vittal K ^a  

^a LAWRENCE BERKELEY NATIONAL LABORATORY   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c TECHNISCHE UNIVERSITÄT BERLIN   (Germany)

^d SLAC NATIONAL ACCELERATOR LABORATORY   (United States)

^e FREIE UNIVERSITÄT BERLIN   (Germany)

^f MAX PLANCK INSTITUTE FOR CHEMICAL ENERGY CONVERSION   (Germany)

^g MAX PLANCK INSTITUTE FOR MEDICAL RESEARCH   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

MANGANESE COMPOUNDS; OXIDATION; PHOTOSYNTHESIS; SINGLE CRYSTALS; X RAY DIFFRACTION;

ANGSTROM-RESOLUTION X-RAY STRUCTURES; EXTENDED X-RAY ABSORPTION FINE STRUCTURE (EXAFS); PHOTOSYSTEM II; PUTATIVE LIGANDS;

WATER;

CALCIUM; MANGANESE; OXYGEN; WATER;

CATALYSIS; CLUSTER ANALYSIS; DATA SET; ELECTRON DENSITY; GEOMETRY; LIGAND; MANGANESE; OXIDATION; PHOTOSYNTHESIS; WATER RESOURCE; X-RAY DIFFRACTION;

ABSORPTION SPECTROPHOTOMETRY; ARTICLE; CATALYSIS; EXTENDED X RAY ABSORPTION FINE STRUCTURE; OXIDATION; PHOTOSYNTHESIS; PHOTOSYSTEM II; POLARIZATION; PRIORITY JOURNAL; X RAY DIFFRACTION;

BINDING SITES; CALCIUM; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; CYANOBACTERIA; FOURIER ANALYSIS; LIGANDS; MANGANESE; MODELS, MOLECULAR; OXIDATION-REDUCTION; OXYGEN; PHOTOSYSTEM II PROTEIN COMPLEX; SPECTRUM ANALYSIS; WATER; X-RAY DIFFRACTION; X-RAYS;

EID: 33750696356     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1128186     Document Type: Article

References (30)

1. T. Wydrzynski, S. Satoh, Photosystem II: The Light-Driven Water: Plastoquinone Oxidoreductase, Advances in Photosynthesis and Respiration Series, vol. 22 (Springer, Dordrecht, Netherlands, 2005).
2. B. Kok, B. Forbush, M. McGloin, Photochem. Photobiol. 11, 457 (1970).
3. T. G. Carrell, A. M. Tyryshkin, G. C. Dismukes, J. Biol. Inorg. Chem. 7, 2 (2002).
4. G. W. Brudvig, Adv. Chem. Ser. 246, 249 (1995).
5. K. Hasegawa, T.-A. Ono, Y. Inoue, M. Kusunoki, Chem. Phys. Lett. 300, 9 (1999).
6. J. M. Peloquin, R. D. Britt, Biochim. Biophys. Acta 1503, 96 (2001).
7. J. Messinger, J. H. A. Nugent, M. C. W. Evans, Biochemistry 36, 11055 (1997).
8. K. A. Áhrling, S. Peterson, S. Styring, Biochemistry 37, 8115 (1998).
9. L. V. Kulik, B. Epel, W. Lubitz, J. Messinger, J. Am. Chem. Soc. 127, 2392 (2005).
10. V. K. Yachandra, K. Sauer, M. P. Klein, Chem. Rev. 96, 2927 (1996).
11. H.-A. Chu, W. Hillier, N. A. Law, G. T. Babcock, Biochim. Biophys. Acta 1503, 69 (2001).
12. A. Zouni et al., Nature 409, 739 (2001).
13. N. Kamiya, J. R. Shen, Proc. Natl. Acad. Sci. U.S.A. 100, 98 (2003).
14. K. N. Ferreira, T. M. Iverson, K. Maghlaoui, J. Barber, S. Iwata, Science 303, 1831 (2004).
15. J. Biesiadka, B. Loll, J. Kern, K. D. Irrgang, A. Zouni, Phys. Chem. Chem. Phys. 6, 4733 (2004).
16. B. Loll, J. Kern, W. Saenger, A. Zouni, J. Biesiadka, Nature 438, 1040 (2005).
17. J. Yano et al., Proc. Natl. Acad. Sci. U.S.A. 102, 12047 (2005).
18. J. H. Robblee et al., J. Am. Chem. Soc. 124, 7459 (2002).
19. R. M. Cinco et al., Biochemistry 41, 12928 (2002).
20. R. M. Cinco et al., Biochemistry 43, 13271 (2004).
21. J. Yano et al., J. Am. Chem. Soc. 127, 14974 (2005).
22. R. A. Scott, J. E. Hahn, S. Doniach, H. C. Freeman, K. O. Hodgson, J. Am. Chem. Soc. 104, 5364 (1982).
23. A. M. Flank, M. Weininger, L. E. Mortenson, S. P. Cramer, J. Am. Chem. Soc. 108, 1049 (1986).
24. Materials and methods are available as supporting material on Science Online.
25. J. J. Rehr, R. C. Albers, Rev. Mod. Phys. 72, 621 (2000).
26. H. A. Chu, W. Millier, R. J. Debus, Biochemistry 43, 3152 (2004).
27. R. J. Debus, M. A. Strickler, L. M. Walker, W. Millier, Biochemistry 44, 1367 (2005).
28. Y. Kimura, N. Mizusawa, T. Yamanari, A. Ishii, T. Ono, J. Biol. Chem. 280, 2078 (2005).
29. Y. Kimura, N. Mizusawa, A. Ishii, T. Ono, Biochemistry 44, 16072 (2005).
30. This work was supported by the Director, the Office of Science, the Office of Basic Energy Sciences (OBES), and the Division of Chemical Sciences, Geosciences, and Biosciences of the U.S. Department of Energy (DOE) under contract DE-AC02-05CH11231; by NIH grant GM 55302; by the Deutsche Forschungsgemeinschaft (grants SFB 498, TP A4, C7, and Me 1629/2-3); and by the Max-Planck-Gesellschaft. Synchrotron facilities were provided by the Stanford Synchrotron Radiation Laboratory (SSRL) operated by DOE OBES. The SSRL Biomedical Technology Program is supported by NIH, the National Center for Research Resources, and the DOE Office of Biological and Environmental Research. We thank E. Berry (Lawrence Berkeley National Laboratory) for help with indexing the PSII XRD pattern and many insights; D. DiFiore and C. Lüneberg for technical assistance; and U. Bergmann (SSRL), S. Un (Commissariat à l'Energie Atomique), and P. Glatzel (European Synchrotron Radiation Facility) for discussions about the analysis of polarization data. We are grateful to M. P. Klein (1921-2000) and H.-T. Witt for their encouragement in initiating this collaborative research.