Functions of cytochrome c in regulation of electron transfer and protein folding.

Published

Journal Article (Review)

Cytochrome c, a "mobile electron carrier" of the mitochondrial respiratory chain, also occurs in detectable amounts in the cytosol, and can receive electrons from cytochromes present in endoplasmic reticulum and plasma membranes as well as from superoxide and ascorbate. The pigment was found to dissociate from mitochondrial membranes in liver and kidney when rats were subjected to heat exposure and starvation, respectively. Treating cytochrome c with hydroxylamine gives a partially deaminated product with altered redox properties; decreased stimulation of respiration by deficient mitochondria, increased reduction by superoxide, and complete loss of reducibility by plasma membranes. Mitochondria isolated from brown adipose tissue of cold-exposed rats are found to be sub-saturated with cytochrome c. The ability of cytochrome c to reactivate reduced ribonuclease is now reinterpreted as a molecular chaperone role for the hemoprotein.

Full Text

Cited Authors

  • Ramasarma, T; Rasheed, BK; Vijaya, S; Puranam, RS; Shivaswamy, V; Gaikwad, AS; Kurup, CK

Published Date

  • April 1, 1992

Published In

Volume / Issue

  • 29 / 2

Start / End Page

  • 173 - 178

PubMed ID

  • 1328035

Pubmed Central ID

  • 1328035

International Standard Serial Number (ISSN)

  • 0301-1208

Language

  • eng

Conference Location

  • India