Ramasarma, T and Rasheed, BK and Vijaya, S and Puranam, RS and Shivaswamy, V and Gaikwad, AS and Kurup, CK (1992) Functions Of Cytochrome-C In Regulation Of Electron-Transfer And Protein Folding. In: Indian Journal of Biochemistry & Biophysics, 29 (2). pp. 173-178.Full text not available from this repository.
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.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to National Institute of Science Communication and Information Resources.|
|Department/Centre:||Division of Biological Sciences > Biochemistry|
|Date Deposited:||02 Apr 2011 05:02|
|Last Modified:||22 Feb 2012 06:11|
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