Thermodynamic and kinetic characterisation of individual haems in multicentre cytochromes c3

Biochimica et Biophysica Acta - Bioenergetics

Volumn 1767, Issue 9, 2007, Pages 1169-1179

  Paquete, Catarina M ^a   Turner, David L ^a,b   Louro, Ricardo O ^a   Xavier, António V ^a   Catarino, Teresa ^a,c  

^a INSTITUTO DE TECNOLOGIA QUÍMICA E BIOLÓGICA   (Portugal)

^b UNIVERSITY OF SOUTHAMPTON   (United Kingdom)

^c UNIVERSIDADE NOVA DE LISBOA   (Portugal)

Author keywords

Cytochrome c3; Desulfovibrio; Electron transfer kinetics; Multicentre protein; Thermodynamic characterisation

Indexed keywords

CYTOCHROME C3; HEMOPROTEIN; PROTON; SODIUM DITHIONITE;

ARTICLE; DESULFOVIBRIO DESULFURICANS; DESULFOVIBRIO GIGAS; DESULFOVIBRIO VULGARIS; ELECTRON; ENZYME KINETICS; FORCE; MICROSCOPY; NUCLEAR MAGNETIC RESONANCE; PKA; PRIORITY JOURNAL; REDUCTION; THERMODYNAMICS;

CYTOCHROME C GROUP; CYTOCHROMES; DESULFOVIBRIO VULGARIS; ELECTRON TRANSPORT; ELECTRONS; HEME; HYDROGEN-ION CONCENTRATION; KINETICS; MAGNETIC RESONANCE SPECTROSCOPY; OXIDATION-REDUCTION; PROTONS; REDUCING AGENTS; SPECTROPHOTOMETRY; TEMPERATURE; THERMODYNAMICS;

DESULFOVIBRIO;

EID: 34548148637     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2007.06.005     Document Type: Article

References (58)

1. Coutinho I.B., and Xavier A.V. Tetraheme cytochromes. Methods Enzymol. 243 (1994) 119-140
2. 3 coupled to hydrogenase works as a 'proton thruster' in Desulfovibrio vulgaris. J. Biol. Inorg. Chem. 2 (1997) 488-491
3. Odom J.M., and Peck Jr. H.D. Hydrogenase, electron-transfer proteins, and energy coupling in the sulfate-reducing bacteria Desulfovibrio. Annu. Rev. Microbiol. 38 (1984) 551-592
4. 3 from Desulfovibrio vulgaris Hildenborough at 1.9 A resolution. J. Mol. Biol. 234 (1993) 680-699
5. 3 from Desulfovibrio desulfuricans Norway at 1.7 A resolution. J. Mol. Biol. 243 (1994) 653-667
6. 3 from Desulfovibrio gigas: crystal structure at 1.8 A resolution and evidence for a specific calcium-binding site. Protein Sci. 5 (1996) 1342-1354
7. 3 from Desulfovibrio africanus. J. Mol. Biol. 290 (1999) 881-902
8. Louro R.O., Bento I., Matias P.M., Catarino T., Baptista A.M., Soares C.M., Carrondo M.A., Turner D.L., and Xavier A.V. Conformational component in the coupled transfer of multiple electrons and protons in a monomeric tetraheme cytochrome. J. Biol. Chem. 276 (2001) 44044-44051
9. Correia I.J., Paquete C.M., Coelho A., Almeida C.C., Catarino T., Louro R.O., Frazão C., Saraiva L.M., Carrondo M.A., Turner D.L., and Xavier A.V. Proton-assisted two-electron transfer in natural variants of tetraheme cytochromes from Desulfomicrobium sp. J. Biol. Chem. 279 (2004) 52227-52237
10. 3 complex: an electron transfer link in the hydrogen-sulfate reduction pathway. J. Mol. Biol. 354 (2005) 73-90
11. 3: structural basis for functional cooperativity. J. Mol. Biol. 281 (1998) 719-739
12. 3 from Desulfovibrio gigas: solution structures of the oxidised and reduced states. J. Mol. Biol. 298 (2000) 61-82
13. 3 from Desulfovibrio desulfuricans Essex 6. Eur. J. Biochem. 268 (2001) 3028-3035
14. 3. Eur. J. Biochem. 141 (1984) 283-296
15. 3 from Desulfovibrio baculatus (DSM 1743). Spectral deconvolution of the heme components. Eur. J. Biochem. 204 (1992) 779-782
16. 3 from Desulfovibrio desulfuricans Norway. Eur. J. Biochem. 177 (1988) 199-206
17. 3 from Desulfovibrio vulgaris Miyazaki. Eur. J. Biochem. 182 (1989) 51-55
18. 3 from Desulfovibrio desulfuricans Norway Strain. Assignment of the heme midpoint redox potentials. J. Mol. Biol. 216 (1990) 161-166
19. 3: new methods of investigation. Biochimie 76 (1994) 524-536
20. Pealing S.L., Cheesman M.R., Reid G.A., Thomson A.J., Ward F.B., and Chapman S.K. Spectroscopic and kinetic studies of the tetraheme flavocytochrome c from Shewanella putrefaciens NCIMB400. Biochemistry 34 (1995) 6153-6458
21. 3 from the thermophilic sulfate reducer Thermodesulfo-bacterium commune. J. Bacteriol. 159 (1984) 1040-1046
22. Moreno C., Campos A., Teixeira M., LeGall J., Montenegro M.I., Moura I., van Dijk C., and Moura J.G. Simulation of the electrochemical behavior of multi-redox systems. Current potential studies on multiheme cytochromes. Eur. J. Biochem. 202 (1991) 385-393
23. 3 from Desulfovibrio vulgaris (Hildenborough). Eur. J. Biochem. 127 (1982) 631-637
24. 3 immobilized on self-assembled monolayers: surface-enhanced resonance Raman spectroscopy and simulation studies. Biophys. J. 88 (2005) 4188-4199
25. 3 and consideration of its properties. Nature 249 (1974) 425-429
26. 3. Biochemistry 13 (1974) 1952-1959
27. 3. Electron transfer mechanisms. Eur. J. Biochem. 127 (1982) 151-155
28. 3 from Desulfovibrio gigas. Eur. J. Biochem. 202 (1991) 1101-1106
29. 3 from Desulfovibrio vulgaris. Eur. J. Biochem. 241 (1996) 723-731
30. 3 from Desulfovibrio gigas: thermodynamics of a "proton thruster". Biochemistry 37 (1998) 15808-15815
31. 3: the importance of mechano-chemical coupling for energy transduction. ChemBioChem 2 (2001) 831-837
32. 3 from Desulfovibrio africanus. Biochim. Biophys. Acta, Bioenerg. 1767 (2007) 178-188
33. 3 from Desulfuromonas acetoxidans. Eur. J. Biochem. 269 (2002) 5722-5730
34. 3 from Desulfovibrio vulgaris. Biochem. Biophys. Res. Commun. 84 (1978) 435-440
35. 3. J. Biochem. 94 (1983) 1375-1385
36. 3 catalyzed by hydrogenase with hydrogen. Biochim. Biophys. Acta 767 (1984) 288-294
37. 3 and ferredoxin from Desulfovibrio desulfuricans Norway strain and their individual reactions with dithionite. Biochim. Biophys. Acta 848 (1986) 279-293
38. 3 and hydrogenase from Desulfovibrio desulfuricans Norway. Biochem. Biophys. Res. Commun. 147 (1987) 1289-1294
39. 3. Eur. J. Biochem. 202 (1991) 1107-1113
40. 3 from Desulfovibrio vulgaris by flash photolysis. Biochim. Biophys. Acta 1140 (1992) 144-156
41. Catarino T., and Turner D.L. Thermodynamic control of electron transfer rates in multicentre redox proteins. ChemBioChem 2 (2001) 416-424
42. 3 from Desulfovibrio vulgaris Miyazaki F. Biophys. J. 85 (2003) 3367-3374
43. Marcus R.A., and Sutin N. Electron transfers in chemistry and biology. Biochim. Biophys. Acta 811 (1985) 265-322
44. 3 by two-dimensional NMR. Eur. J. Biochem. 210 (1992) 931-936
45. Dutton P.L. Redox potentiometry: determination of midpoint potentials of oxidation-reduction components of biological electron-transfer systems. Methods Enzymol. 54 (1978) 411-435
46. McKenna C.E., Gutheil W.G., and Song W. A method for preparing analytically pure sodium dithionite. Dithionite quality and observed nitrogenase-specific activities. Biochim. Biophys. Acta 1075 (1991) 109-117
47. Dixon M. The acceptor specificity of flavins and flavoproteins: I. Techniques for anaerobic spectrophotometry. Biochim. Biophys. Acta 226 (1971) 241-258
48. Lambeth D.O., and Palmer G. The kinetics and mechanism of reduction of electron transfer proteins and other compounds of biological interest by dithionite. J. Biol. Chem. 248 (1973) 6095-6103
49. 3 from Desulfovibrio vulgaris. Eur. J. Biochem. 244 (1997) 721-734
50. - in aqueous-solutions-Pulse radiolytic and cyclic voltammetric studies. J. Phys. Chem. 91 (1987) 1606-1611
51. Christiansen H.E.M., Coutinho I., Conrad L.S., Hammerstad-Pedersen J.M., Iversen G., Jensen M.H., Karlsson J.J., Ulstrup J., and Xavier A.V. Electron transport networks in multicentre metalloproteins. J. Photochem. Photobiol. 82 (1994) 103-115
52. Moss G.P. Nomenclature of tetrapyrroles. Recommendations 1986. IUPAC-IUB Joint Commission on Biochemical Nomenclature (JCBN). Eur. J. Biochem. 178 (1988) 277-328
53. 3 from several Desulfovibrio species using continuum electrostatic methods. J. Biol. Inorg. Chem. 4 (1999) 73-86
54. 3 from D. vulgaris Miyazaki F on the basis of its reduced solution structure. J. Mol. Biol. 319 (2002) 767-778
55. Page C.C., Moser C.C., Chen X., and Dutton P.L. Natural engineering principles of electron tunnelling in biological oxidation-reduction. Nature 402 (1999) 47-52
56. Tollin G., Hanson L.K., Caffrey M., Meyer T.E., and Cusanovich M.A. Redox pathways in electron-transfer proteins: correlations between reactivities, solvent exposure, and unpaired-spin-density distributions. Proc. Natl. Acad. Sci. U. S. A. 83 (1986) 3693-3697
57. Shulman R.G., Glarum S.H., and Karplus M. Electronic structure of cyanide complexes of hemes and heme proteins. J. Mol. Biol. 57 (1971) 93-115
58. Turner D.L., Salgueiro C.A., Schenkels P., LeGall J., and Xavier A.V. Carbon-13 NMR studies of the influence of axial ligand orientation on haem electronic structure. Biochim. Biophys. Acta 1246 (1995) 24-28