Literature summary extracted from
Page, T.R.; Hoffman, B.M.
Control of cyclic photoinitiated electron transfer between cytochrome c peroxidase (W191F) and cytochrome c by formation of dynamic binary and ternary complexes (2015), Biochemistry, 54, 1188-1197 .
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
1.11.1.5 |
W191F |
mutation eliminates electron fast hole hopping through residue W191, enhancing accumulation of charge-separated intermediate and extending the timescale for binding/dissociation of the charge-separated complex. The photocycle includes dissociation/recombination of the charge-separated binary complex and a charge-separated ternary complex, [Zn-protoporphyrin+CcP, Fe2+cytochrome c, Fe3+cytochrome] |
Saccharomyces cerevisiae |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
1.11.1.5 |
Saccharomyces cerevisiae |
P00431 |
- |
- |
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
1.11.1.5 |
cytochrome c |
thermodynamic affinity constants for binding the first and second cytochrome c are KI 0.0000001 per M, KII 0.0001 per M. Cytochrome c binds at the weaker-binding site with relatively great affinity, and places upper bounds on the contributions of repulsion between the two cytochrome c of the ternary complex |
Saccharomyces cerevisiae |
|