Literature summary for 1.11.1.5 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 .

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Protein Variants

Protein Variants	Comment	Organism
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

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	P00431	-	-

Cofactor

Cofactor	Comment	Organism	Structure
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

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Release 2023.1 (January 2023)