The polarity of tyrosine 67 in yeast iso-1-cytochrome c monitored by second derivative spectroscopy

Biochemistry and Cell Biology

Volumn 75, Issue 3, 1997, Pages 191-197

  Schroeder, Hans R ^a,c   McOdimba, Francis A ^a,d   Guy Guillemette, J ^b   Kornblatt, Jack A ^a  

^a Dept of Electrical and Computer Engineering   (Canada)

^b UNIVERSITY OF WATERLOO   (Canada)

^c MCGILL UNIVERSITY   (Canada)

^d INTERNATIONAL LIVESTOCK RESEARCH INSTITUTE   (Kenya)

Author keywords

Crevice; Derivative spectroscopy; Heme; Mutagenesis; Water

Indexed keywords

CYC1 PROTEIN, S CEREVISIAE; CYTOCHROME C; SACCHAROMYCES CEREVISIAE PROTEIN; TYROSINE;

ANIMAL; ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYMOLOGY; GENETICS; HORSE; HYDROGEN BOND; OXIDATION REDUCTION REACTION; PROTEIN TERTIARY STRUCTURE; SACCHAROMYCES CEREVISIAE; SITE DIRECTED MUTAGENESIS; ULTRAVIOLET SPECTROPHOTOMETRY;

ANIMALS; CYTOCHROME C GROUP; CYTOCHROMES C; HORSES; HYDROGEN BONDING; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; OXIDATION-REDUCTION; PROTEIN STRUCTURE, TERTIARY; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SPECTROPHOTOMETRY, ULTRAVIOLET; TYROSINE;

EID: 0031303978     PISSN: 08298211     EISSN: None     Source Type: Journal    
DOI: 10.1139/o97-036     Document Type: Article

References (15)

1. Atkins, W.M., and Sligar, S.G. 1990. Tyrosine-96 as a natural spectroscopic probe of the cytochrome p-450cam active site. Biochemistry, 29: 1271-1275.
2. Balestrieri, C., Colonna, G., Giovane, A., Irace, G., and Servillo, L. 1978. Second derivative spectroscopy of proteins: a method for the quantitative determination of aromatic amino acids in proteins. Eur. J. Biochem. 90: 433-440.
3. Balestrieri, C., Colonna, G., Giovane, A., Irace, G., and Servillo, L. 1980. Second derivative spectroscopy of proteins: studies on tyrosyl residues. Anal. Biochem. 106: 49-54.
4. Berguis, A.M. 1992. Ph.D thesis, University of British Columbia, Vancouver, B.C.
5. Berguis, A.M., and Brayer, G.D. 1992. Oxidation state-dependent conformational changes in cytochrome c. J. Mol. Biol. 223: 959-976.
6. Berguis, A.M., Guillemette, J.G., Smith, M., and Brayer, G.D. 1994a. Mutation of tyrosine-67 in cytochrome c significantly alters the local heme environment. J. Mol. Biol. 235: 1326-1341.
7. Berguis, A.M., Guillemette, J.G., McLendon, G., Sherman, F., Smith, M., and Brayer, G.D. 1994b. The role of a conserved internal water molecule and its associated hydrogen bond network in cytochrome c. J. Mol. Biol. 236: 786-799.
8. Buckle, A.M., Cramer, P., and Fersht, A.R. 1996. Structural and energetic responses to cavity-creating mutations in hydrophobic cores: observations of a buried water molecule and the hydrophilic nature of such hydrophobic cavities. Biochemistry, 35: 4298-4305.
9. Bushnell, G.W., Louie, G.V., and Brayer, G.D. 1990. High-resolution three-dimensional structure of horse heart cytochrome c. J. Mol. Biol. 214: 585-595.
10. Cutler, R.L., Pielak, G.J., Mauk, A.G., and Smith, M. 1987. Replacement of cysteine-107 of Saccharomyces cerevisiae iso-1-cytochrome c with threonine: improved stability of the mutant protein. Protein Eng. 1: 95-99.
11. Davies, A.M., Guillemette, J.G., Smith, M., and Moore, G.R. 1993. Redesign of the interieur hydrophilic region of mitochondrial cytochrome c by site-directed mutagenesis. Biochemistry, 32: 5431-5435.
12. Dunitz, J.D. 1994. The entropic cost of bound water in crystals and biomolecules. Science (Washington, D.C.), 264: 670.
13. Faye, G., Leung, D.W., Tatchel, K., Hall, B.D., and Smith, M. 1981. Deletion mapping of sequences essential for in vivo transcription of the iso-1-cytochrome c gene. Proc. Natl. Acad. Sci. U.S.A. 78: 2258-2262.
14. Fisher, M.T., and Sligar, S.G. 1985. Tyrosine motions in relation to the ferric spin equilibrium of cytochrome P-450cam. Biochemistry, 24: 6696-6701.
15. Fisher, M.T., and Stadtman, E.R. 1992. Oxidative modification of Escherichia coli glutamine synthetase. J. Biol. Chem. 267: 1872-1880.