Increasing the redox potential of isoform 1 of yeast cytochrome c through the modification of select haem interactions

Biochemical Journal

Volumn 362, Issue 2, 2002, Pages 281-287

  Lett, C Marc ^a   Guillemette, J Guy ^a  

^a UNIVERSITY OF WATERLOO   (Canada)

Author keywords

Formal potential; Mutagenesis; Spectroscopy

Indexed keywords

ADSORPTION; MUTAGENS; OXIDATION; PROTEINS; SPECTROSCOPIC ANALYSIS; YEAST;

REDOX POTENTIAL;

BIOCHEMISTRY;

CYTOCHROME C; MUTANT PROTEIN;

ARTICLE; OXIDATION REDUCTION POTENTIAL; OXIDATIVE PHOSPHORYLATION; POINT MUTATION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN PURIFICATION; PROTEIN STABILITY; PROTEIN STRUCTURE; SPECTROSCOPY;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BINDING SITES; CIRCULAR DICHROISM; CYTOCHROME C GROUP; CYTOCHROMES C; ELECTROCHEMISTRY; HEME; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; OXIDATION-REDUCTION; PROTEIN CONFORMATION; PROTEIN ISOFORMS; RECOMBINANT PROTEINS; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SPECTROPHOTOMETRY;

EUKARYOTA;

EID: 0036499923     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/0264-6021:3620281     Document Type: Article

References (36)

1. A theoretical model for the effects of local nonpolar heine environments on the redox potentials in cytochromes
2. Haem exposure as the determinate of oxidation-reduction potential of haem proteins
3. Structural basis for the variation in redox potential of cytochromes
4. Coupling between oxidation state and hydrogen bond conformation in heme proteins
5. Control of redox properties of cytochrome c by special electrostatic interactions
6. Axial ligand replacement in horse heart cytochrome c by semisynthesis
7. Semisynthesis of axial-ligand (position 80) mutants in cytochrome c
8. Structurally engineered cytochromes with novel ligand-binding sites: Oxy and carbon monoxy derivatives of semisynthetic horse heart Ala80 cytochrome c
9. A method of directed random mutagenesis of the yeast chromosome shows that the iso-1-cytochrome c heme ligand His18 is essential
10. Functional role of heme ligation in cytochrome c. Effects of replacement of methionine 80 with natural and non-natural residues by semisynthesis
11. Structural significance of an internal water molecule studied by site-directed mutagenesis of tyrosine-67 in rat cytochrome c
12. Substitutions engineered by chemical synthesis at three conserved sites in mitochondrial cytochrome c. Thermodynamic and functional consequences
13. The role of a conserved internal water molecule and its associated hydrogen bond network in cytochrome c
14. Mutation of tyrosine-67 to phenylalanine in cytochrome c significantly alters the local heme environment
15. Changing the invariant proline-30 of rat and Drosophila melanogaster cytochromes c to alanine or valine destabilizes the heme crevice more than the overall conformation
16. Redesign of the interior hydrophilic region of mitochondrial cytochrome c by site-directed mutagenesis
17. Change in charge of an unvaried heme contact residue does not cause a maior change of conformation in cytochrome c
18. Tuning the redox potential of cytochrome c through synergistic site replacement
19. Analysis of the invariant Phe82 residue of yeast iso-1-cytochrome c by site-directed mutagenesis using a phagemid yeast shuttle vector
20. 5 through mutagenesis and molecular modelling
21. Replacement of cysteine-107 of Saccharomyces cerevisiae iso-1-cytochrome c with threonine: Improved stability of the mutant protein
22. Electrochemical, kinetic, and circular dichroic consequences of mutations at position 82 of yeast iso-1-cytochrome c
23. Deletion mapping of sequences essential for in vivo transcription of the iso-1-cytochrome c gene
24. 551
25. A study of cytochrome c haemochromogen
26. Mutants of yeast defective in iso-1-cytochrome c
27. Mechanistic and structural contributions of critical surface and internal residues to cytochrome c electron transfer reactivity
28. A study on the role of evolutionarily invariant leucine 32 of cytochrome c
29. High-resolution refinement of yeast iso-1-cytochrome c and comparisons with other eukaryotic cytochromes c
30. Horse heart cytochrome c. The oxidation-reduction potential and protein structures
31. Conformation of cytochromes. 3. Effect of urea, temperature, extrinsic ligands, and pH variation on the conformation of horse heart ferricytochrome c.
32. Identification of Lys79 as an iron ligand in one form of alkaline yeast iso-1-ferricytochrome c
33. Amino acid replacements in yeast iso-1-cytochrome c. Comparison with the phylogenetic series and the tertiary structure of related cytochromes c
34. Oxidation state-dependent conformational changes in cytochrome c