Importance of the region including aspartates 57 and 60 of ferredoxin on the electron transfer complex with photosystem I in the cyanobacterium Synechocystis sp. PCC 6803

Biochemical and Biophysical Research Communications

Volumn 271, Issue 3, 2000, Pages 647-653

  Guillouard, Isabelle ^a   Lagoutte, Bernard ^a   Moal, Gweénaeëlle ^a   Bottin, Herveé ^a  

^a DIF   (France)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; ARGININE; ASPARTIC ACID; CYSTEINE; FERREDOXIN; LYSINE; MUTANT PROTEIN;

ABSORPTION SPECTROSCOPY; AMINO ACID SUBSTITUTION; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; CYANOBACTERIUM; DISSOCIATION CONSTANT; ELECTRON TRANSPORT; ESCHERICHIA COLI; PHOTOSYSTEM I; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN PROTEIN INTERACTION;

ESCHERICHIA COLI; SYNECHOCYSTIS; SYNECHOCYSTIS SP.; SYNECHOCYSTIS SP. PCC 6803;

EID: 0034685627     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1006/bbrc.2000.2687     Document Type: Article

References (38)

1. Knaff, D. B., and Hirasawa, M. (1991) Ferredoxin-dependent chloroplast enzymes. Biochim. Biophys. Acta 1056, 93-125.
2. Knaff, D. B. (1996) Ferredoxin and ferredoxin-dependent enzymes. In Oxygenic Photosynthesis: The Light Reactions (Ort, D. R., and Yocum, C. F., Eds.), pp. 333-361, Kluwer Academic, Dordrecht.
3. + reductase: site-directed mutagenesis and laser flash photolysis. Biochemistry 32, 9346-9354.
4. + reductase. J. Am. Chem. Soc. 115, 11698-11701.
5. Golbeck, J. H. (1994) Photosystem I in cyanobacteria. in Advances in Photosynthesis, The Molecular Biology of Cyanobacteria (Bryant, D. A., Ed.) pp. 319-360, Kluwer Academic Publishers, Dordrecht, The Netherlands.
6. Sétif, P., and Bottin H. (1994) Laser flash absorption spectroscopy study of ferredoxin reduction by photosystem I in Synechocystis sp. PCC 6803: Evidence for submicrosecond and microsecond kinetics. Biochemistry 33, 8495-8504.
7. Sétif, P., and Bottin H. (1995) Laser flash absorption spectroscopy study of ferredoxin reduction by photosystem I: Spectral and kinetic evidence for the existence of several photosystem I-ferredoxin complexes. Biochemistry 34, 9059-9070.
8. Zanetti, G., and Merati, G. (1987) Interaction between photosystem I and ferredoxin: Identification by chemical cross-linking of the polypeptide which binds ferredoxin. Eur. J. Biochem. 169, 143-146.
9. Zilber, A. L., and Malkin, R. (1988) Ferredoxin cross-links to a 22 kDa subunit of photosystem I. Plant Physiol. 88, 810-814.
10. Lelong, C., Sétif, P., Lagoutte, B., and Bottin, H. (1994) Identification of the amino acids involved in the functional interaction between photosystem I and ferredoxin from Synechocystis sp. PCC 6803 by chemical cross-linking. J. Biol. Chem. 269, 10034-10039.
11. Fischer, N., Hippler, M., Sétif, P., Jacquot, J.-P., and Rochaix, J.-D. (1998) The PsaC subunit of photosystem I provides an essential lysine residue for fast electron transfer to ferredoxin. EMBO J. 17, 849-858.
12. Lelong, C., Boekema, E. J., Kruip, J., Bottin, H., Rogner, M., and Sétif, P. (1996) Characterization of a redox active cross-linked complex between cyanobacterial photosystem I and soluble ferredoxin. EMBO J. 15, 2160-2168.
13. Kruip, J., Chitnis, P. R., Lagoutte, B., Rogner, M., and Boekema, E. J. (1997) Structural Organization of the Major Subunits in Cyanobacterial Photosystem 1. Localization of subunits PsaC, -D, -E, -F, and -J. J. Biol. Chem. 272, 17061-17069.
14. Rousseau, F., Sétif, P., and Lagoutte, B. (1993) Evidence for the involvement of PSI-E in the reduction of ferredoxin by photosystem I. EMBO J. 12, 1755-1765.
15. Xu, Q., Jung, Y.-S., Chitnis, V. P., Guikema, J. A., Golbeck, J. H., and Chitnis, P. R. (1994) Mutational analysis of photosystem I polypeptides in Synechocystis sp. PCC 6803. Subunit requirements for reduction of NADP+ mediated by ferredoxin and flavodoxin. J. Biol. Chem. 269, 21512-21518.
16. Hanley, J., Sétif, P., Bottin, H., and Lagoutte, B. (1996) Mutagenesis of photosystem I in the region of the ferredoxin cross-linking site: Modifications of the positively charged amino acids. Biochemistry 35, 8563-8571.
17. Klukas, O., Schubert, W.-D., Jordan, P., Krauss, N., Fromme, P., Witt, H. T., and Saenger, W. (1999) Photosystem I, an improved model of the stromal subunits PsaC, PsaD, and PsaE. J. Biol. Chem. 274, 7351-7360.
18. Chitnis, V. P., Jung, Y.-S., Albee, L., Golbeck, J. H., Chitnis, P. R. (1996) Mutational analysis of photosystem I polypeptides. J. Biol. Chem. 271, 11772-11780.
19. Barth, P., Guillouard, I., Sétif, P., and Lagoutte, B. (2000) Essential role of a single arginine of photosystem I in stabilizing the electron transfer complex with ferredoxin. J. Biol. Chem. 275, 7030-7036.
20. + reductase, and cytochrome c. Arch. Biochem. Biophys. 321, 229-238.
21. Poncelet, M., Cassier-Chauvat, C., Leschelle, X., Bottin, H., and Chauvat, F. (1998) Targeted deletion and mutational analysis of the essential (2Fe-2S) plant-like ferredoxin in Synechocystis PCC6803 by plasmid shuffling. Mol. Microbiol. 28, 813-821.
22. B is the immediate electron donor to soluble ferredoxin. Biochemistry 37, 3429-3439.
23. Barth, P., Lagoutte, B., and Sétif, P. (1998) Ferredoxin reduction by photosystem I from Synechocystis sp. PCC 6803: Toward an understanding of the respective roles of subunits PsaD and PsaE in ferredoxin binding. Biochemistry 46, 16233-16241.
24. Tsukihara, T., Fukuyama, K., Nakamura, M., Katsube, Y., Tanaka, N., Kakudo, M., Wada, K., Hase, T., and Matsubara, H. (1981) X-ray analysis of a [2Fe-2S] ferredoxin from Spirulina platensis. Main chain fold and location of side chains at 2.5 Å resolution. J. Biochem. (Tokyo) 90, 1763-1773.
25. + reductase: The role of carboxyl groups, electrostatic surface potential, and molecular dipole moment. Protein Science 2, 1126-1135.
26. Jacquot, J.-P., Stein, M., Suzuki, A., Liottet, S., Sandoz, G., and Miginiac-Maslow, M. (1997) Residue Glu-91 of Chlamydomonas reinhardtii ferredoxin is essential for electron transfer to ferredoxin-thioredoxin reductase. FEBS Lett. 400, 293-296.
27. Bottin, H., and Lagoutte, B. (1992) Ferredoxin and flavodoxin from the cyanobacterium Synechocystis sp PCC 6803. Biochim. Biophys. Acta 1101, 48-56.
28. 15N NMR sequential assignement, secondary structure, and tertiary fold of [2Fe-2S] ferredoxin from Synechocystis sp. PCC 6803. Biochemistry 34, 14462-14473.
29. X) from the cyanobacterium Synechocystis PCC 6803 J. Biol. Chem. 268, 23353-23360.
30. Mathis, P., and Sétif, P. (1981) Near infra-red absorption spectra of the chlorophyll a cations and triplet state in vitro and in vivo. Isr. J. Chem. 21, 316-320.
31. Brandt, M. E., and Vickery, L. E. (1993) Charge pair interactions stabilizing ferredoxin-ferredoxin reductase complexes. J. Biol. Chem. 268, 17126-17130.
32. + photoreduction. Eur. J. Biochem. 236, 465-469.
33. + reductase for site-specific ferredoxin mutants. Biochemistry 36, 11100-11117.
34. Vieira, B. J., Colvert, K. K., and Davis, D. J. (1986) Chemical modification and cross-linking as probes of regions on ferredoxin involved in the interaction with ferredoxin:NADP reductase. Biochim. Biophys. Acta 851, 109-122.
35. + oxidoreductase. Biochemistry 27, 3753-3759.
36. Schmitz, S., and Böhme, H. (1995) Amino acid residues involved in functional interaction of vegetative cell ferredoxin from the cyanobacterium Anabaena sp. PCC 7120 with ferredoxin:NADP reductase, nitrite reductase and nitrate reductase. Biochim. Biophys. Acta 1231, 335-341.
37. García-Sánchez, M. I., Gotor, C., Jacquot, J.-P., Stein, M., Suzuki, A., and Vega, J. M. (1997) Critical residues of Chlamydomonas reinhardtii ferredoxin for interaction with nitrite reductase and glutamate synthase revealed by site-directed mutagenesis. Eur. J. Biochem. 250, 364-368.
38. Aliverti, A., Livraghi, A., Piubelli, L., and Zanetti, G. (1997) On the role of the acidic cluster Glu 92-94 of spinach ferredoxin I. Biochim. Biophys. Acta 1342, 45-50.