Rate constant for interaction of cytochrome c with cytochrome c peroxidase and with cytochrome b5
| Range | 10^7 - 10^9 M^-1×sec^-1 |
|---|---|
| Organism | Various |
| Reference | Northrup SH, Erickson HP. Kinetics of protein-protein association explained by Brownian dynamics computer simulation. Proc Natl Acad Sci U S A. 1992 Apr 15 89(8):3338-42. p.3338 left column bottom paragraphPubMed ID1565624 |
| Primary Source | [7] Kang, C. H., Brautigan, D. L., Osheroff, N. & Margoliash, E. (1978) Definitaion of cytochrome c binding domains by chemical modification. Reaction of carboxydinitrophenyl- and trinitrophenyl-cytochromes c with baker's yeast cytochrome c peroxidase. J. Biol. Chem. 253, 6502-6510. [8] Eltis, L. D., Herbert, R. G., Barker, P. D., Mauk, A. G. & Northrup, S. H. (1991) Reduction of horse heart ferricytochrome c by bovine liver ferrocytochrome b5. Experimental and theoretical analysis. Biochemistry 30, 3663-3674.PubMed ID210187, 1849735 |
| Method | Primary source [8] abstract: "The reduction of horse heart ferricytochrome c by the tryptic fragment of bovine liver cytochrome b5 and its dimethyl ester heme (DME)-substituted derivative has been studied as a function of ionic strength, pH, and temperature under solution conditions where the reaction is bimolecular." |
| Comments | p.3338 left column bottom paragraph: "Faster bimolecular rates have been reported (BNID 112540) for insulin dimerization (k2 = 10^8 M^-1×s^-1) and for interaction of cytochrome c with cytochrome c peroxidase (primary source 7) and cytochrome b5 (primary source 8) (k2 varies from 10^7 to 10^9, with the faster rates at low ionic strength). These very fast reactions are the results of strong attractive coulombic forces that highly favor formation of the productive reaction complexes (primary source 8, refs 9-11)." Primary source [7] studied horse and yeast. Primary source [8] studied horse and cow |
| Entered by | Uri M |
| ID | 112541 |