Multiple orientations in a physiological complex: The pyruvate-ferredoxin oxidoreductase-ferredoxin system

Biochemistry

Volumn 43, Issue 49, 2004, Pages 15480-15493

  Pieulle, Laetitia ^a   Nouailler, Matthieu ^a   Morelli, Xavier ^a   Cavazza, Christine ^a,c   Gallice, Philippe ^b   Blanchet, Stéphane ^a   Bianco, Pierre ^a   Guerlesquin, Françoise ^a   Hatchikian, E Claude ^a  

^a CNRS   (France)

^b INSTITUT DE BIOLOGIE STRUCTURALE   (France)

^c AIX MARSEILLE UNIVERSITY   (France)

Author keywords

[No Author keywords available]

Indexed keywords

CALORIMETRY; ELECTRON TRANSITIONS; ELECTROSTATICS; HYDROPHOBICITY; IONIC STRENGTH; METABOLISM; MUTAGENESIS; NUCLEAR MAGNETIC RESONANCE; REACTION KINETICS; REDOX REACTIONS; THERMODYNAMIC PROPERTIES;

BINDING AFFINITY; ELECTRON TRANSFER; PYRUVATE-FERREDOXIN OXIDOREDUCTASE (PFOR);

ENZYME KINETICS;

BACTERIAL PROTEIN; CARBOXYLIC ACID; FERREDOXIN; PYRUVATE SYNTHASE;

ANAEROBIC BACTERIUM; ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; DESULFOVIBRIO; DESULFOVIBRIO AFRICANUS; ELECTRICITY; ELECTRON TRANSPORT; ENERGY METABOLISM; IONIC STRENGTH; KINETICS; MICROCALORIMETRY; MUTAGENESIS; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; NUCLEOTIDE SEQUENCE; OXIDATION REDUCTION REACTION; PHYSIOLOGY; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; THERMODYNAMICS;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BINDING SITES; CALORIMETRY; CLONING, MOLECULAR; DESULFOVIBRIO AFRICANUS; ELECTRON TRANSPORT; ELECTROSTATICS; ENERGY METABOLISM; ENZYME STABILITY; FERREDOXINS; HYDROPHOBICITY; KETONE OXIDOREDUCTASES; MACROMOLECULAR SUBSTANCES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PYRUVATE SYNTHASE; SURFACE PROPERTIES; THERMODYNAMICS;

BACTERIA (MICROORGANISMS); DESULFOVIBRIO; DESULFOVIBRIO AFRICANUS; NEGIBACTERIA;

EID: 10644272614     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0485878     Document Type: Article

References (57)

1. Evans, M. C. W., Buchanan, B. B., and Arnon, D. I. (1966) A new-ferredoxin-dependent carbon reduction cycle in a photosynthetic bacterium, Proc. Natl. Acad. Sci. U.S.A. 55, 928-934.
2. Tersteegen, A., Linder, D., Thauer, R. K., and Hedderich, R. (1997) Structures and functions of four anabolic 2-oxoacid oxidoreductases in Methanobacterium thermoautotrophicum. Eur. J. Biochem. 242, 862-868.
3. Chabrière, E., Charon, M.-H., Volbeda, A., Pieulle, L., Hatchikian, E. C., and Fontecilla-Camps, J.-C. (1999) Crystal structure of pyruvate:ferredoxin oxidoreductase, a central enzyme in anaerobic metabolism, and its complex with pyruvate, Nat. Struct. Biol. 6, 182-190.
4. Pieulle, L., Guigliarelli, B., Asso, M., Dole, F., Bernadac, A., and Hatchikian, E. C. (1995) Isolation and characterization of the pyruvate:ferredoxin oxidoreductase from the sulfate-reducing bacterium Desulfovibrio africanus, Biochim. Biophys. Acta 1250, 49-59.
5. Moser, C. C., Keske, J. M., Farid, R. S., and Dutton, P. L. (1992) Nature of biological electron transfer, Nature 355, 796-802.
6. Pieulle, L., Charon, M.-H., Bianco, P., Bonicel, J., Pétillot, Y., and Hatchikian, E. C. (1999) Structural and kinetic studies of the pyruvate:ferredoxin oxidoreductase/ferredoxin complex from Desulfovibrio africanus, Eur. J. Biochem. 264, 500-508.
7. Sery, A., Housset, D., Serre, L., Bonicel, J., Hatchikian, E. C., Frey, M., and Roth, M. (1994) Crystal structure of the ferredoxin I from Desulfovibrio africanus at 2.3 Å resolution, Biochemistry 33, 15408-15417.
8. 1H NMR spectroscopy and comparison of its solution structure with its crystal structure, J. Mol. Biol. 277, 683-706.
9. Bendall, D. S. (1996) Interprotein electron transfer, in Protein Electron Transfer (Bendall, D. S., Ed.) pp 43-68, BIOS Scientific Publishers, Oxford, U.K.
10. Morelli, X., Palma, P. N., Krippahl, L., Guerlesquin, F., and Rigby, A. C. (2001) A novel approach for assessing macromolecular complexes combining soft-docking calculations with NMR data, Protein Sci. 10, 2131-2137.
11. Pieulle, L., Magro, V., and Hatchikian, E. C. (1997) Isolation and analysis of the gene encoding the pyruvate:ferredoxin oxidoreductase of Desulfovibrio africanus, production of the recombinant enzyme in Escherichia coli, and effect of carboxy-terminal deletions on its stability, J. Bacteriol. 179, 5684-5692.
12. Nakamura, M., Saeki, K., and Takahashi, Y. (1999) Hyperproduction of recombinant ferredoxins in Escherichia coli by coexpression of the ORF1-ORF2-iscS-iscU-iscA-hscB-hscA-fdx-ORF3 gene cluster, J. Biochem. 126, 10-18.
13. Hatchikian, E. C., Jones, H. E., and Bruschi, M. (1979) Isolation and characterization of a rubredoxin and two ferredoxins from Desulfovibrio africanus, Biochim. Biophys. Acta 548, 471-483.
14. LeGall, J., and Forget, N. (1978) Purification of electron-transfer components from sulfate-reducing bacteria, Methods Enzymol. 53, 613-634.
15. Papavassiliou, P., and Hatchikian, E. C. (1985) Isolation and characterization of a rubredoxin and a two-(4Fe-4S) ferredoxin from Thermodesulfobacterium commune, Biochim. Biophys. Acta 810, 1-11.
16. Guerlesquin, F., Bruschi, M., Bovier-Lapierre, G., and Fauque, G. (1980) Comparative studies of two ferredoxins from Desulfovibrio desulfuricans Norway, Biochim. Biophys. Acta 626, 127-135.
17. Laemmli, U. K. (1970) Cleavage of structural proteins during assembly of the head of bacteriophage T4, Nature 227, 680-685.
18. Crestfield, A. M., Moore, S., and Stein, W. H. (1963) The preparation and enzymatic hydrolysis of reduced and S-carboxymethylated proteins, J. Biol. Chem. 238, 622-627.
19. 3 and ferredoxin from Desulfovibrio desulfuricans Norway strain and their individual reactions with dithionite, Biochim. Biophys. Acta 848, 279-293.
20. Cleland, W. W. (1967) The statistical analysis of enzyme kinetic data, Adv. Enzymol. 29, 1-32.
21. Haladjian, J., Thierry-Chef, I., and Bianco, P. (1996) Permselective-membrane pyrolytic graphite electrode for the study of microvolumes of [2Fe-2S] ferredoxin, Talanta 43, 1125-1130.
22. Palma, P. N., Krippahl, L., Wampler, J. E., and Moura, J. J. G. (2000) BiGGER: a new (soft) docking algorithm for predicting protein interactions, Proteins 39, 372-384.
23. 553-ferredoxin complex, Biochemistry 39, 2530-2537.
24. Kauzmann, W. (1959) Some factors in the interpretation of protein denaturation, Adv. Protein Chem. 14, 1-63.
25. Hatchikian, E. C., Cammack, R., Patil, D. S., Robinson, A. E., Richards, A. J. M., George, S., and Thomson, A. J. (1984) Spectroscopic characterization of ferredoxin I and II from Desulfovibrio africanus, Biochim. Biophys. Acta 784, 40-47.
26. 2+/+ cluster reduction potential, J. Biol. Chem. 269, 8564-8575.
27. Pettigrew, G. W., Goodhew, C. F., Cooper, A., Nutley, M., Jumel, K., and Harding, S. E. (2003) The electron-transfer complexes of cytochrome c peroxidase from Paracoccus denitrificans, Biochemistry 42, 2046-2055.
28. Chothia, C., and Janin, J. (1975) Principles of protein-protein recognition, Nature 256, 705-708.
29. Pelletier, H., and Kraut, J. (1992) Crystal structure of a complex between electron-transfer partners, cytochrome c peroxidase and cytochrome c, Science 258, 1748-1755.
30. Garrett, D. S., Seok, Y. J., Peterkofsky, A., Clore, G. M., and Gronenborn, A. M. (1997) Identification by NMR of the binding surface for the histidine-containing phosphocarrier protein HPr on the N-terminal domain of enzyme I of the Escherichia coli phosphotransferase system, Biochemistry 36, 4393-4398.
31. LoConte, L., Chothia, C., and Janin, J. (1999) The atomic structure of protein-protein recognition sites, J. Mol. Biol. 285, 2177-2198.
32. Morales, R., Charon, M.-H., Kachalova, G., Serre, L., Medina, M., Gomez-Moreno, C., and Frey, M. (2000) A redox-dependent interaction between two electron-transfer partners involved in photosynthesis, EMBO Rep. 1, 271-276.
33. 553 complex combining transverse relaxation-optimized spectroscopy experiments and soft docking calculations, J. Biol. Chem. 275, 23204-23210.
34. 3-[Fe]- hydrogenase electron-transfer complex: structural model by NMR restrained docking, FEBS Lett. 548, 1-4.
35. Bianco, P., Haladjian, J., Manjaoui, A., and Bruschi, M. (1988) Electrochemical study of flavin mononucleotide and of flavodoxin from Desulfovibrio vulgaris Hildenborough. Electrochim. Acta 33, 745-752.
36. Kissinger, C. R., Sieker, L. C., Adman, E. T., and Jensen, L. H. (1991) Refined crystal structure of ferredoxin II from Desulfovibrio gigas at 1.7 Å, J. Mol. Biol. 219, 693-715.
37. Cammack, R., Rao, K. K., and Bargeron, C. P. (1977) Midpoint redox potentials of plant and algal ferredoxins, Biochem. J. 168, 205-209.
38. Meyer, J., Clay, M. D., Johnson, M. K., Stubna, A., Münck, E., Higgins, C., and Wittung-Stafshede, P. (2002) A hyperthermophilic plant-type [2Fe-2S] ferredoxin from Aquifex aeolicus is stabilized by a disulfide bond, Biochemistry 41, 3096-3108.
39. Wahl, R. C., and Orme-Johnson, W. H. (1987) Clostridial pyruvate oxidoreductase and the pyruvate-oxidizing enzyme specific to nitrogen fixation in Klebsiella pneumoniae are similar enzymes, J. Biol. Chem. 262, 10489-10496.
40. Knight, E., Jr., and Hardy, R. W. F. (1966) Isolation and characteristics of flavodoxin from nitrogen-fixing Clostridium pasteurianum, J. Biol. Chem. 241, 2752-2756.
41. Akagi, J. M. (1967) Electron carriers for the phosphoroclastic reaction of Desulfovibrio desulfuricans, J. Biol. Chem. 242, 2478-2483.
42. Dubourdieu, M., and LeGall, J. (1970) Chemical study of two flavodoxins extracted from sulfate reducing bacteria, Biochem. Biophys. Res. Commun. 38, 965-972.
43. Hatchikian, E. C., and LeGall, J. (1970) (Study of dicarboxylic acid and pyruvate metabolism in sulfate-reducing bacteria. II. Electron transport; final acceptors), Ann. Inst. Pasteur 118, 288-301.
44. Crowley, P. B., Vintonenko, N., Bullerjahn, G. S., and Ubbink, M. (2002) Plastocyanin-cytochrome f interactions: the influence of hydrophobic patch mutations studied by NMR spectroscopy, Biochemistry 41, 15698-15705.
45. Moulis, J.-M., and Davasse, V. (1995) Probing the role of electrostatic forces in the interaction of Clostridium pasteurianum ferredoxin with its redox partners, Biochemistry 34, 16781-16788.
46. Brereton, B. S., Maher, M. J., Tregloan, P. A., and Wedd, A. G. (1999) Investigation of the role of surface residues in the ferredoxin from Clostridium pasteurianum, Biochim. Biophys. Acta 1429, 307-316.
47. Fukuyama, K., Matsubara, H., Tsukihara, T., and Katsube, Y. (1989) Structure of [4Fe-4S] ferredoxin from Bacillus thermoproteolyticus refined at 2.3 Å resolution, J. Mol. Biol 210, 383-398.
48. Nicolet, Y., Piras, C., Legrand, P., Hatchikian, E. C., and Fontecilla-Camps, J.-C. (1999) Desulfovibrio desulfuricans iron hydrogenase: the structure shows unusual coordination to an active site Fe binuclear center, Structure 7, 13-23.
49. Coghlan, V. M., and Vickery, L. E. (1991) Site-specific mutations in human ferredoxin that affect binding to ferredoxin reductase and cytochrome P450scc, J. Biol. Chem. 266, 18606-18612.
50. + reductase system from Anabaena, Biochimie 77, 539-548.
51. + reductase system from Anabaena, Biochimie 80, 837-846.
52. Chen, L., Durkey, R., Poliks, B. J., Hanada, K., Chen, Z., Mathews, F. S., Davidson, V. L., Satow, Y., Huizinga, E., Vellieux, F. M. D., and Hol, W. G. (1992) Crystal structure of an electron-transfer complex between methylamine dehydrogenase and amicyanin, Biochemistry 31, 4959-4964.
53. Hu, Y., Faham, S., Roy, R., Adams, M. W. W., and Rees, D. C. (1999) Formaldehyde ferredoxin oxidoreductase from Pyrococcus furiosus: The 1.85 Å resolution crystal structure and its mechanistic implications, J. Mol. Biol. 286, 899-914.
54. 5: A nuclear magnetic resonance study of a highly dynamic protein complex, Biochemistry 41, 11721-11730.
55. Menon, A. L., Hendrix, H., Hutchins, A., Verhagen, M. F. J. M., and Adams, M. W. W. (1998) The δ-subunit of pyruvate ferredoxin oxidoreductase from Pyrococcus furiosus is a redox-active, iron-sulfur protein: evidence for an ancestral relationship with 8Fe-type ferredoxins, Biochemistry 37, 12838-12846.
56. LeGall, J., and Fauque, G. (1988) Dissimilatory reduction of sulfur compounds, in Biology of Anaerobic Microorganisms (Zehnder, A. J. B., Ed.) pp 587-639, John Wiley and Sons, New York.
57. Kremer, D. R., Nienhuis-Kuiper, H. E., Timmer, C. J., and Hansen, T. A. (1989) Catabolism of malate and related dicarboxylic acids in various Desulfovibrio strains and the involvement of an oxygen-labile NADPH dehydrogenase. Arch. Microbiol 151, 34-39.