THE ROLE OF A CONSERVED INTERNAL WATER MOLECULE AND ITS ASSOCIATED HYDROGEN BOND NETWORK IN CYTOCHROME C
THE HEME GROUP IS COVALENTLY ATTACHED TO THE PROTEIN VIA THIOETHER BONDS TO THE SG ATOMS OF CYS 14 AND CYS 17.
Mutation of Tyrosine-67 in Cytochrome C Significantly Alters the Local Heme Environment
Effect of the Asn 52-> Ile Mutation on the Redox Potential of Yeast Cytochrome C: Theory and Experiment
Oxidation State-Dependent Conformational Changes in Cytochrome C
Enhanced Thermodynamic Stabilities of Yeast Iso-1-Cytochrome C with Amino Acid Replacements at Position 52 and 102
Effects of Reaction Free Energy in Biological Electron Transfer in Vitro and in Vivo (in: Electron Transfer in Inorganic, Organic, and Biological Systems)
High-Resolution Refinement of Yeast Iso-1-Cytochrome C and Comparisons with Other Eukaryotic Cytochromes C
Crystallization of Yeast Iso-2-Cytochrome C Using a Novel Hair Seeding Technique
TEFKAGSAKKGATLFKTRCLQCHTVEKGGPHKVGPNLHGIFGRHSGQAEGYSYTDAIIKKNVLWDENNMSEFLTNP (M3L)KYIPGTKMAFGGLKKEKDRNDLITYLKKATE
TEFKAGSAKKGATLFKTRCLQCHTVEKGGPHKVGPNLHGIFGRHSGQAEGYSYTDAIIKKNVLWDENNMSEFLTNPKKYI PGTKMAFGGLKKEKDRNDLITYLKKATE
HELIX THE END OF THE 50 HELIX (RESIDUE 55) IS DISTORTED.
SHEET RESIDUES IN SHEET S1 FORM A HIGHLY DISTORTED BETA TYPE CONFORMATION.
THIS PROTEIN HAS BEEN STABILIZED FOR ANALYSES BY THE MUTATION OF CYSTEINE 102 TO A THREONINE RESIDUE. IN TURN T5 THE H-BOND IS MEDIATED THROUGH A WATER MOLECULE.
CYTOCHROME C (ISOZYME 1) (REDUCED) MUTANT WITH ASN 52 REPLACED BY ILE, TYR 67 REPLACED BY PHE, AND CYS 102 REPLACED BY THR (N52I,Y67F,C102T)
TEFKAGSAKKGATLFKTRCLQCHTVEKGGPHKVGPNLHGIFGRHSGQAEGYSYTDANIKKNVLWDENNMSEYLTNPKKYI PGTKMAFGGLKKEKDRNDLITYLKKACE