Protein-protein interaction in electron transfer reactions: The ferredoxin/flavodoxin/ferredoxin:NADP+ reductase system from Anabaena

Biochimie

Volumn 80, Issue 10, 1998, Pages 837-846

  Gómez Moreno, Carlos ^a   Martínez Júlvez, Marta ^a   Medina, Milagros ^a   Hurley, John K ^b   Tollin, Gordon ^b  

^a UNIVERSITY OF ZARAGOZA   (Spain)

^b University of Arizona   (United States)

Author keywords

Ferredoxin; Flavodoxin; FNR; Protein protein interaction

Indexed keywords

FERREDOXIN; FERREDOXIN NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE REDUCTASE; FLAVODOXIN;

ANABAENA; COMPLEX FORMATION; CONFERENCE PAPER; CONTROLLED STUDY; ELECTRON TRANSPORT; ENZYME STRUCTURE; MOLECULAR STABILITY; NONHUMAN; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; STRUCTURE ACTIVITY RELATION;

ANABAENA; BACTERIA (MICROORGANISMS); CYANOBACTERIA;

EID: 0032181129     PISSN: 03009084     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0300-9084(00)88878-1     Document Type: Conference Paper

References (50)

1. + oxidoreductase from Anabaena, FEBS Lett. 170 (1984) 85-88.
2. + oxidoreductase and flavodoxin from Anabaena PCC 7119 and their electrostatic complexes, Eur. J. Biochem. 202 (1991) 1065-1071.
3. [3] Rogers L.J., Ferredoxins, flavodoxins and related proteins: structure, function and evolution, in: Fay P., Van Baalen C. (Eds.), The Cyanobacteria, Elsevier, 1987, pp. 35-67.
4. + binding at 2.25 Å resolution, J. Mol. Biol. 263 (1996) 20-39.
5. [5] Rypniewski W.R., Breiter D.R., Benning M.M., Wesenberg G., Oh, B.H., Markley J.L., Rayment I., Holden H.M., Crystallisation and structure determination to 2.5 Å resolution of the oxidised [2Fe-2S] ferredoxin isolated from Anabaena 7120, Biochemistry 30 (1991) 4126-4131.
6. [6] Rao S.T., Shaffie F., Yu C., Satyshur K.A., Stockman B.J., Markley J.L., Sundaralingan M., Structure of the oxidised long-chain flavodoxin from Anabaena 7120 at 2 Å resolution, Protein Sci. 1 (1992) 1413-1427.
7. + reductase: prototype for a structurally novel flavoenzyme family, Science 251 (1991) 60-66.
8. [8] Rossman M., Moras D., Olsen K., Chemical and biological evolution of a nucleotide-binding protein, Nature 250 (1974) 194-199.
9. [9] Bruns C.M., Karplus P.A., Refined crystal structure of spinach ferredoxin reductase at 1. 7 Å resolution: oxidised, reduced and 2′-phospho-5′-AMP bound states, J. Mol. Biol. 247 (1995) 125-145.
10. [10] Correll C.C., Ludwig M.L., Bruns C.M., Karplus P.A., Structural prototypes from an extended family of flavoprotein reductases: comparison of phthalate dioxygenase reductase with ferredoxin reductase and ferredoxin, Protein Sci. 2 (1993) 2112-2133.
11. [11] Karplus P.A., Bruns C.M., Structure-function relations for ferredoxin reductase, J. Bioenerg. Biomembr. 26 (1994) 89-99.
12. + reductase. Differential chemical modification of free and ferredoxin:bound enzyme, Eur. J. Biochem. 216 (1993) 57-66.
13. + reductase, Biochemistry 27 (1988) 3753-3759.
14. + reductase from Anabaena sp. PCC 7119 involved in substrate binding, FEBS Lett. 298 (1992) 25-28.
15. + reductase from Anabaena sp. PCC 7119 to its substrates, Arch. Biochem. Biophys. 299 (1992) 281-286.
16. + reductase, J. Biol. Chem. 259 (1984) 6153-6157.
17. + reductase in the interaction with ferredoxin, FEBS Lett. 343 (1994) 247-250.
18. + reductase with ferredoxin probed by site directed mutagenesis, Biochim. Biophys. Acta 1363 (1998) 85-93.
19. + reductase: site-directed mutagenesis and laser flash photolysis, Biochemistry 32 (1993) 9346-9354.
20. + reductase, J. Am. Chem. Soc. 115 (1993) 11698-11701.
21. + reductase system from Anabaena: requirement of a negative charge at position 94 in ferredoxin for rapid electron transfer, Arch. Biochem. Biophys. 312 (1994) 480-486.
22. + reductase system from Anabaena, Biochimie 77 (1995) 539-548.
23. + reductase by altering protein/protein orientation within the intermediate complex, Arch. Biochem. Biophys. 333 (1996) 243-250.
24. + reductase from Anabaena PCC 7119, Biochemistry 37 (1998) 2715-2728.
25. [25] Alam J., Whitaker R.A., Krogman D.W., Curtis S.E., Isolation and sequence of the gene for ferredoxin I from the cyanobacterium Anabaena sp. strain PCC 7120, J. Bacteriol. 168 (1986) 1265-1271.
26. + reductase gene from Anabaena PCC 7119, Nucleic Acids Res. 18 (1990) 7161.
27. [27] Gómez-Moreno C., Martínez-Júlvez M., Fillat M.F., Hurley J.K., Tollin G., Molecular recognition in electron transfer proteins, in: Mathis P. (Ed.), Photosynthesis: from Light to Biosphere, Kluwer Academic Publishers, the Netherlands, II, 1995, pp. 627-632.
28. [28] Fillat M.F., Borrias W.E., Weisbeek P.J., Isolation and overexpression in Escherichia coli of the flavodoxin gene from Anabaena PCC 7119, Biochem. J. 280 (1991) 187-191.
29. + reductase from Anabaena with its substrates, Arch. Biochem. Biophys. 288 (1991) 231-238.
30. [30] Bhattacharyya A.K., Tollin G., Davis M., Edmondson D.E., Laser flash photolysis studies of intramolecular electron transfer in milk xanthine oxidase, Biochemistry 22 (1983) 5270-5279.
31. + reductase system from Anabaena, J. Am. Chem. Soc. 118 (1996) 5526-5531.
32. + reductase and free flavins. Electron transfer within a protein-protein complex, J. Biol. Chem. 260 (1985) 1452-1458.
33. [33] Tollin G., Use of laser flash photolysis time-resolved spectrophotometry to investigate interprotein and intraprotein electron transfer mechanisms, J. Bioenerg. Biomembr. 27 (1995) 303-309.
34. [34] Tollin G., Hazzard J.T., Intra-and intermolecular electron transfer processes in redox proteins, Arch. Biochem. Biophys. 287 (1991) 1-7.
35. [35] Tollin G., Hurley J.K., Hazzard J.T., Meyer T.E., Use of laser flash photolysis time-resolved spectrophotometry to investigate interprotein and intraprotein electron transfer mechanisms, Biophys. Chem. 48 (1993) 259-279.
36. [36] Simondsen R.P., Tollin G., Transient kinetics of redox reactions of flavodoxin: effects of chemical modification of the flavin mononucleotide prosthetic group on the dynamics of intermediate complex formation and electron transfer, Biochemistry 22 (1983) 3008-3016.
37. [37] Van Der Plas J., De Groot R.P., Weisbeek P.J., VanArkel G.A., Coding sequence of a ferredoxin gene from Anabaena variabilis ATCC 29413, Nucleic Acids Res. 14 (1986) 7803.
38. [38] Reith M.E., Laudenbach D.E., Straus N.A., Isolation and nucleotide sequence analysis of the ferredoxin I gene from the cyanobacterium Anacystis nidulans R2., J. Bacteriol. 168 (1986) 1319-1324.
39. [39] Böhme H., Haselkorn R., Molecular cloning and nucleotide sequence analysis of the gene coding for heterocyst ferredoxin from the cyanobacterium Anabaena sp. strain PCC 7120, Mol. Gen. Genet. 214 (1988) 278-285.
40. + reductase and the role of water at the complex interface, Biochemistry 33 (1994) 13321-13328.
41. + reductase, Eur. J. Biochem. 203 (1992) 373-379.
42. + reductases from Anabaena PCC 7119 and spinach, Arch. Biochem. Biophys. 287 (1991) 351-358.
43. + reductase for site-specific ferredoxin mutants, Biochemistry 36 (1997) 11100-11117.
44. + reductase, and cytochrome c, Arch. Biochem. Biophys. 321 (1995) 229-238.
45. [45] Qin L., Kostic N.M., Enforced interaction of one molecule of plastocyanin with two molecules of cytochrome c and an electrontransfer reaction involving the hydrophobic patch on the plastocyanin surface, Biochemistry 35 (1996) 3379-3386.
46. [46] Ubbink M., Ejdeback M., Karsson B.C., Bendall D.S., The structure of the complex of plastocyanin and cytochrome f, determined by paramagnetic NMR and restrained rigid-body molecular dynamics, Structure 6 (1998) 323-335.
47. [47] Coghlan V.M., Vickery L.E., Electrostatic interactions stabilising ferredoxin electron transfer complexes, J. Biol. Chem. 267 (1992) 8932-8935.
48. [48] Corin A.F., McLendon G., Zang Q., Hake R.A., Falvo J., Lu K.S., Ciccarelli R.B., Holzschu B., Effects of surface amino acid replacements in cytochrome c peroxidase on complex formation with cytochrome c, Biochemistry 30 (1991) 11585-11595.
49. [49] Jenkins C.M., Genzor C.G., Fillat M.F., Waterman M.R., Gómez-Moreno C., Negatively charged Anabaena flavodoxin residues (Asp144 and Glu145) are important for reconstitution of cytochrome P450 17α-hydroxylase activity, J. Biol. Chem. 272 (1997) 22509-22513.
50. [50] Naud I., Meyer C., David L., Breton J., Gaillard J., Jouanneau Y., Identification of residue of Rhodobacter capsulatus ferredoxin I important for its interaction with nitrogenase, Eur. J. Biochem. 237 (1996) 399-405.