Detecting transient protein-protein interactions by X-ray absorption spectroscopy: The cytochrome c6-photosystem I complex

FEBS Letters

Volumn 580, Issue 13, 2006, Pages 3023-3028

  Díaz Moreno, Irene ^a   Díaz Quintana, Antonio ^a   Subías, Gloria ^b   Mairs, Trevor ^c   De la Rosa, Miguel A ^a   Díaz Moreno, Sofía ^d  

^a UNIVERSITY OF SEVILLE   (Spain)

^b UNIVERSITY OF ZARAGOZA   (Spain)

^c EUROPEAN SYNCHROTRON RADIATION FACILITY   (France)

^d DIAMOND LIGHT SOURCE LTD   (United Kingdom)

Author keywords

Cytochrome c6; Photosystem I; Transient interactions; X ray absorption spectroscopy

Indexed keywords

CYTOCHROME C6; FERROUS ION; HEME; IRON; METALLOPROTEIN;

ABSORPTION SPECTROSCOPY; ARTICLE; GEOMETRY; NONHUMAN; OXIDATION; OXIDATION REDUCTION STATE; PHOTOSYSTEM I; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FUNCTION; PROTEIN ISOLATION; PROTEIN PROTEIN INTERACTION; ROENTGEN SPECTROSCOPY;

CYTOCHROMES C6; ESCHERICHIA COLI PROTEINS; PHOTOSYSTEM I PROTEIN COMPLEX; PROTEIN INTERACTION MAPPING; SPECTRUM ANALYSIS; X-RAYS;

EID: 33646575279     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2006.04.045     Document Type: Article

References (26)

1. Hasnain S.S., and Strange R.W. Marriage of XAFS and crystallography for the structure-function studies of metalloproteins. J. Synchroton Rad. 10 (2003) 9-15
2. Hasnain S.S. Synchroton techniques for metalloproteins and human disease in post-genome era. J. Synchroton Rad. 11 (2004) 7-11
3. 6-photosystem I case. J. Biol. Chem. 280 (2005) 7925-7931
4. Korszun Z.R., Moffat K., Frank K., and Cusanovich M.A. Extended X-ray absorption fine structure studies of cytochromes c: Structural aspects of oxidation-reduction. Biochemistry 21 (1982) 2253-2258
5. Cheng M.G., Rich A.M., Armstrong R.S., Ellis P.J., and Lay P.A. Determination of iron-ligand bond lengths in ferric and ferrous horse heart cytochrome c using multiple-scattering analyses of XAFS data. Inorg. Chem. 38 (1999) 5703-5708
6. 6 from the cyanobacterium Anabaena sp. PCC 7119. Biochem. Biophys. Res. Commun. 243 (1998) 302-306
7. Fujii T., Yokoyama E., Inoue K., and Sakurai H. The sites of electron donation of photosystem I to methyl viologen. Biochim. Biophys. Acta 1015 (1990) 41-48
8. B is the immediate electron donor to soluble ferredoxin. Biochemistry 37 (1998) 3429-3439
9. 6 photooxidation by photosystem I particles. Eur. J. Biochem. 213 (1993) 1133-1138
10. Filipponi A., Di Cicco A., De Panfilis S., Trapananti A., Itiè J.-P., Borowski M., and Ansell S. An experimental station for advanced research on condensed matter under extreme conditions at the European synchrotron radiation facility - BM29 beamline. Rev. Sci. Instrum. 71 (2000) 2422-2432
11. Koningsberger D.C., and Prins R. X-ray absorption: Principles, Application, Techniques of EXAFS, SEXAFS and XANES (1988), Wiley, New York, USA
12. Rehr J.J., Zabinsky S.I., and Alberts R.C. High-order multiple-scattering calculations of X-ray-absorption fine structure. Phys. Rev. Lett. 69 (1992) 3397-3401
13. Newville M. IFEFFIT: interactive XAFS analysis and FEFF fitting. J. Synchrotron Rad. 8 (2001) 322-324
14. Ravel, B. and Newville, M. Athena and Artemis: interactive graphical data analysis using Ifeffit. J. Synchrotron Rad. 12, 537-541.
15. Westre T.E., Kennepohl P., DeWitt J.G., Hedman B., Hodgson K.O., and Solomon E.I. A multiplet analysis of Fe K-edge 1s → 3d pre-edge features of iron complexes. J. Am. Chem. Soc. 119 (1997) 6297-6314
16. Labhardt A., and Yuen C. X-ray absorption edge fine structure spectroscopy of the active site haem of cytochrome c. Nature 277 (1979) 150-151
17. Levina A., Armstrong R.S., and Lay P.A. Three-dimensional structure determination using multiple-scattering analysis of XAFS: applications to metalloproteins and coordination chemistry. Coord. Chem. Rev. 249 (2005) 141-160
18. Korszun Z.R., Bunker G., Khalid S., Scheidt W.R., Cusanovich M.A., and Meyer T.E. Extended X-ray absorption fine structure study of Rhodospirillum rubrum and Rhodospirillum molischianum cytochromes c: Relationship between heme stereochemistry and spin state. Biochemistry 28 (1989) 1513-1517
19. Hoard J.L. Stereochemistry of hemes and other metalloproteins. Science 174 (1971) 1295-1302
20. Mauk A.G., and Moore G.R. Control of metalloprotein redox potentials: What does site-directed mutagenesis of hemoproteins tell us?. J. Biol. Inorg. Chem. 2 (1997) 119-125
21. Rompel A., Cinco R.M., Robblee J.H., Latimer M.J., McFarlane K.L., Huang J., Walters M.A., and Yachandra V.K. S K- and Mo L-edge X-ray absorption spectroscopy to determine metal-ligand charge distribution in molybdenum-sulfur compounds. J. Synchroton Rad. 8 (2001) 1006-1008
22. 2 and the photosynthetic reaction center of Rhodobacter sphaeroides. Biochemistry 36 (1997) 1418-1427
23. 3: influence of cytochrome c and carbon monoxide on the midpoint potential values. Biochemistry 16 (1977) 4966-4971
24. 2: reaction center electron transfer complex from Rhodobacter sphaeroides. Photosynth. Res. 85 (2005) 101-114
25. 550 in the cyanobacterium Thermosynechococcus elongatus. J. Biol. Inorg. Chem. 8 (2003) 206-216
26. Dolla A., Blanchard L., Guerlesquin F., and Bruschi M. The protein moiety modulates the redox potential in cytochromes c. Biochimie 76 (1994) 471-479