Protein dynamics in the region of the sixth ligand methionine revealed by studies of imidazole binding to Rhodobacter capsulatus cytochrome c2 hinge mutants

Biochemistry

Volumn 43, Issue 24, 2004, Pages 7717-7724

  Dumortier, C ^a   Fitch, J ^a   Van Petegem, F ^b   Vermeulen, W ^b   Meyer, T E ^a   Van Beeumen, J J ^b   Cusanovich, M A ^a  

^a UNIVERSITY OF ARIZONA   (United States)

^b GHENT UNIVERSITY   (Belgium)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BACTERIA; CONFORMATIONS; MOLECULAR STRUCTURE; MUTAGENESIS; REACTION KINETICS;

CYTOCHROMES; LIGANDS;

PROTEINS;

CYTOCHROME C2; HEME; IMIDAZOLE; IRON; LIGAND; METHIONINE; PROTEIN; SULFUR;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; BACTERIUM MUTANT; BINDING KINETICS; CARBOXY TERMINAL SEQUENCE; CONFORMATIONAL TRANSITION; ENZYME BINDING; ENZYME KINETICS; ENZYME STRUCTURE; LIGAND BINDING; MOLECULAR DYNAMICS; MUTATIONAL ANALYSIS; NONHUMAN; OXIDATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN PROTEIN INTERACTION; RHODOBACTER CAPSULATUS;

CYTOCHROMES C2; IMIDAZOLES; KINETICS; LIGANDS; METHIONINE; MUTATION; RHODOBACTER CAPSULATUS;

BACTERIA (MICROORGANISMS); RHODOBACTER; RHODOBACTER CAPSULATUS; RHODOPSEUDOMONAS;

EID: 2942709817     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0362370     Document Type: Article

References (17)

1. Schejter, A., and Aviram, I. (1969) The reaction of cytochrome c with imidazole, Biochemistry 8, 149-153.
2. Sutin, N., and Yandell, J. K. (1972) Mechanisms of the reactions of cytochrome c. Rate and equilibrium constants for ligand binding to horse heart ferricytochrome c, J. Biol. Chem. 247, 6932-6936.
3. Dumortier, C., Meyer, T. E., and Cusanovich, M. A. (1999) Protein dynamics: Imidazole binding to class I c-type cytochromes, Arch. Biochem. Biophys. 371, 142-148.
4. 2. Effect of site-directed mutants on ligand binding, J. Biol. Chem. 273, 25647-25653.
5. 2 from Rhodobacter sphaeroides in three crystal forms, Acta Crystallogr. D50, 596-602.
6. Berghuis, A. M., Guillemette, J. G., McLendon, G., Sherman, F., Smith, M., and Brayer, G. D. (1994) The role of a conserved internal water molecule and its associated hydrogen bond network in cytochrome c, J. Mol. Biol. 236, 786-799.
7. Banci, L., Bertini, I., Liu, G., Lu, J., Reddig, T., Tang, W., Wu, Y., Yao, Y., and Zhu, D. (2001) Effects of extrinsic imidazole ligation on the molecular and electronic structure of cytochrome c, J. Biol. Inorg. Chem. 6, 628-637.
8. 2 mutant, glycine 95 proline, Arch. Biochem. Biophys. 405, 154-162.
9. Caffrey, M., Davidson, E., Cusanovich, M. A., and Daldal, F. (1992) Cytochrome c2 mutants of Rhodobacter capsulatus, Arch. Biochem. Biophys. 292, 419-426.
10. 2 isolated from Rhodobacter capsulatus determined at 2.5 A resolution, J. Mol. Biol. 220, 673-685.
11. Leys, D., Backers, K., Meyer, T. E., Hagen, W. R., Cusanovich, M. A., and Van Beeumen, J. J. (2000) Crystal structures of an oxygen-binding cytochrome c from Rhodobacter sphaeroides, J. Biol. Chem. 275, 16050-6.
12. Louie, G. V., and Brayer, G. D. (1989) A polypeptide chain refolding event occurs in the Gly82 variant of yeast iso-1 cytochrome c, J. Mol. Biol. 209, 313-322.
13. Louie, G. V., Pielak, G. J., Smith, M., and Brayer, G. D. (1988) Role of phenylalanine-82 in yeast iso-1-cytochrome c and remote conformational changes induced by a serine residue at this position, Biochemistry 27, 7870-7876.
14. Rafferty, S. P., Pearce, L. L., Barker, P. D., Guillemette, J. G., Kay, C. M., Smith, M., and Mauk, A. G. (1990) Electrochemical, kinetic, and circular dichroic consequences of mutations at position 82 of yeast iso-1 cytochrome c, Biochemistry 29, 9365-9369.
15. Concar, D. W., Whitford, D., Pielak, G. J., and Williams, R. J. P. (1991) The role of phenylalanine-82 in electron exchange reactions of eukaryotic cytochromes c, J. Am. Chem. Soc. 113, 2401-2406.
16. Lo, T. P., Guillemette, J. G., Louie, G. V., Smith, M., and Brayer G. D. (1995) Structural studies of the roles of residues 82 and 85 at the interactive face of cytochrome c, Biochemistry 34, 163-171.
17. Feinberg B. A., Liu, X., Ryan, M. D., Schejter, A., Zhang, C., and Margoliash, E. (1998) Direct voltammetric observation of redox driven changes in axial coordination and intramolecular rearrangement of the phenylalanine-82 histidine variant of yeast iso-1 cytochrome c, Biochemistry 37, 13091-13101.