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Lakshmi KV, Reifler MJ, Chisholm DA, et al. Correlation of the cytochrome c (550) content of cyanobacterial Photosystem II with the EPR properties of the oxygen-evolving complex. Photosynth Res. 2002;72(2):175-89doi: 10.1023/A:1016140902662.
Lakshmi, K. V., Reifler, M. J., Chisholm, D. A., Wang, J. Y., Diner, B. A., & Brudvig, G. W. (2002). Correlation of the cytochrome c (550) content of cyanobacterial Photosystem II with the EPR properties of the oxygen-evolving complex. Photosynthesis research, 72(2), 175-89. https://doi.org/10.1023/A:1016140902662
Lakshmi, K V, et al. "Correlation of the cytochrome c (550) content of cyanobacterial Photosystem II with the EPR properties of the oxygen-evolving complex." Photosynthesis research vol. 72,2 (2002): 175-89. doi: https://doi.org/10.1023/A:1016140902662
Lakshmi KV, Reifler MJ, Chisholm DA, Wang JY, Diner BA, Brudvig GW. Correlation of the cytochrome c (550) content of cyanobacterial Photosystem II with the EPR properties of the oxygen-evolving complex. Photosynth Res. 2002;72(2):175-89. doi: 10.1023/A:1016140902662. PMID: 16228516.
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Photosynth Res. 2002;72(2):175-89. doi: 10.1023/A:1016140902662.

Correlation of the cytochrome c (550) content of cyanobacterial Photosystem II with the EPR properties of the oxygen-evolving complex.

Photosynthesis research

K V Lakshmi, Michael J Reifler, Dexter A Chisholm, Jamie Y Wang, Bruce A Diner, Gary W Brudvig

Affiliations

  1. Department of Chemistry, Yale University, New Haven, CT, 06520-8107, USA, [email protected].

PMID: 16228516 DOI: 10.1023/A:1016140902662

Abstract

The Mn(4) cluster of PS II advances through a series of oxidation states (S states) that catalyze the breakdown of water to dioxygen in the oxygen-evolving complex. The present study describes the engineering and purification of highly active PS II complexes from mesophilic His-tagged Synechocystis PCC 6803 and purification of PS II core complexes from thermophilic wild-type Synechococcus lividus with high levels of the extrinsic polypeptide, cytochrome c (550). The g = 4.1 S(2) state EPR signal, previously not characterized in untreated cyanobacterial PS II, is detected in high yields in these PS II preparations. We present a complete characterization of the g = 4.1 state in cyanobacterial His-tagged Synechocystis PCC 6803 PS II and S. lividus PS II. Also presented are a determination of the stoichiometry of cytochrome c (550) bound to His-tagged Synechocystis PCC 6803 PS II and analytical ultracentrifugation results which indicate that cytochrome c (550) is a monomer in solution. The temperature-dependent multiline to g = 4.1 EPR signal conversion observed for the S(2) state in cyanobacterial PS II with high cytochrome c (550) content is very similar to that previously found for spinach PS II. In spinach PS II, the formation of the S(2) state g = 4.1 EPR signal has been found to correlate with the binding of the extrinsic 17 and 23 kDa polypeptides. The finding of a similar correlation in cyanobacterial PS II with the binding of cytochrome c (550) suggests a functional homology between cytochrome c (550) and the 17 and 23 kDa extrinsic proteins of spinach PS II.

References

  1. J Biol Inorg Chem. 2001 Mar;6(3):324-32 - PubMed
  2. Biochemistry. 2000 Nov 14;39(45):13788-99 - PubMed
  3. Biochim Biophys Acta. 1974 Jun 28;347(3):439-42 - PubMed
  4. Biochemistry. 1994 Apr 19;33(15):4594-603 - PubMed
  5. Biochemistry. 1993 Feb 23;32(7):1825-32 - PubMed
  6. Biochemistry. 1998 Jun 23;37(25):8995-9000 - PubMed
  7. FEBS Lett. 1994 Nov 28;355(2):121-4 - PubMed
  8. Photosynth Res. 1986 Jan;10(3):393-403 - PubMed
  9. J Biol Inorg Chem. 2001 Sep;6(7):708-16 - PubMed
  10. Biochemistry. 1996 Jun 4;35(22):6984-9 - PubMed
  11. Nucleic Acids Res. 1988 Jan 11;16(1):358 - PubMed
  12. Biochemistry. 1999 Mar 30;38(13):4072-7 - PubMed
  13. Photosynth Res. 1990 Apr;24(1):1-13 - PubMed
  14. Biochemistry. 1988 May 31;27(11):4021-31 - PubMed
  15. Proc Natl Acad Sci U S A. 1981 Jan;78(1):274-8 - PubMed
  16. Biochemistry. 2001 Aug 7;40(31):9215-25 - PubMed
  17. Biochemistry. 1996 Nov 12;35(45):14259-67 - PubMed
  18. Biochemistry. 1992 Feb 25;31(7):2099-107 - PubMed
  19. Nature. 2001 Feb 8;409(6821):739-43 - PubMed
  20. Biochim Biophys Acta. 1991 Jan 3;1056(1):1-18 - PubMed
  21. Biochemistry. 1986 Oct 21;25(21):6487-94 - PubMed
  22. Biochemistry. 1994 Apr 12;33(14):4393-400 - PubMed
  23. Gene. 1989 Apr 15;77(1):61-8 - PubMed
  24. Biochim Biophys Acta. 1992 Jan 30;1099(1):25-34 - PubMed
  25. Eur J Biochem. 1999 Dec;266(2):453-9 - PubMed
  26. Biochemistry. 1985 Dec 31;24(27):8114-20 - PubMed
  27. Biochim Biophys Acta. 1998 Nov 2;1409(1):50-7 - PubMed
  28. Biochemistry. 1998 Jul 14;37(28):10040-6 - PubMed
  29. Biochemistry. 1991 Apr 23;30(16):3943-50 - PubMed
  30. J Biol Chem. 1995 Mar 24;270(12):6901-7 - PubMed
  31. Photochem Photobiol. 1970 Jun;11(6):457-75 - PubMed
  32. J Biol Chem. 1990 Apr 15;265(11):6189-96 - PubMed
  33. Biochemistry. 1998 Mar 24;37(12):4001-7 - PubMed
  34. Biochemistry. 2000 May 9;39(18):5246-54 - PubMed
  35. J Am Chem Soc. 1997 Nov;119(46):11349-11350 - PubMed
  36. Biochim Biophys Acta. 1992 Oct 16;1102(3):269-352 - PubMed
  37. Biochemistry. 1998 Apr 14;37(15):5039-45 - PubMed
  38. Photosynth Res. 2000;66(3):189-98 - PubMed
  39. Plant Physiol. 1994 Aug;105(4):1313-9 - PubMed
  40. Biochemistry. 1995 Oct 3;34(39):12661-8 - PubMed
  41. Biochemistry. 1997 Sep 23;36(38):11351-9 - PubMed
  42. FEBS Lett. 1998 Apr 10;426(1):140-4 - PubMed
  43. Biochim Biophys Acta. 2000 Apr 21;1457(3):145-56 - PubMed
  44. Plant Cell Physiol. 1999 Dec;40(12):1219-31 - PubMed
  45. FEBS Lett. 1992 Apr 20;301(2):145-9 - PubMed
  46. Anal Biochem. 1976 Sep;75(1):168-76 - PubMed
  47. Biochemistry. 1997 Oct 28;36(43):13148-52 - PubMed

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