Issue 30, 2009

Tyrosine-67 in cytochrome c is a possible apoptotic trigger controlled by hydrogen bonds via a conformational transition

Abstract

We found that cyt c Y67H and Y67R variants represent a state which resembles the conformational intermediate state in cyt c with high peroxidase activity; and also the hydrogen bond network around Tyr67 is associated with the conformational transition of cyt c; these suggest that the hydrogen bond network around Tyr67 is essential in maintaining the cyt c functioning not only as an electron transfer protein but also probably as a trigger in apoptosis.

Graphical abstract: Tyrosine-67 in cytochrome c is a possible apoptotic trigger controlled by hydrogen bonds via a conformational transition

Supplementary files

Article information

Article type
Communication
Submitted
03 Mar 2009
Accepted
15 Jun 2009
First published
29 Jun 2009

Chem. Commun., 2009, 4512-4514

Tyrosine-67 in cytochrome c is a possible apoptotic trigger controlled by hydrogen bonds via a conformational transition

T. Ying, Z. Wang, Y. Lin, J. Xie, X. Tan and Z. Huang, Chem. Commun., 2009, 4512 DOI: 10.1039/B904347K

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