The reaction of neuroglobin with potential redox protein partners cytochrome b5 and cytochrome c
- 10 August 2006
- journal article
- Published by Wiley in FEBS Letters
- Vol. 580 (20) , 4884-4888
- https://doi.org/10.1016/j.febslet.2006.08.003
Abstract
Previously identified, potentially neuroprotective reactions of neuroglobin require the existence of yet unknown redox partners. We show here that the reduction of ferric neuroglobin by cytochrome b 5 is relatively slow (k = 6 × 102 M−1 s−1 at pH 7.0) and thus is unlikely to be of physiological significance. In contrast, the reaction between ferrous neuroglobin and ferric cytochrome c is very rapid (k = 2 × 107 M−1 s−1) with an apparent overall equilibrium constant of 1 μM. Based on this data we propose that ferrous neuroglobin may well play a role in preventing apoptosis.Keywords
This publication has 35 references indexed in Scilit:
- Suppression of the pro-apoptotic function of cytochrome c by singlet oxygen via a haem redox state-independent mechanismBiochemical Journal, 2005
- Allosteric Regulation and Temperature Dependence of Oxygen Binding in Human Neuroglobin and CytoglobinJournal of Biological Chemistry, 2004
- Dissociation of Cytochrome c from the Inner Mitochondrial Membrane during Cardiac IschemiaJournal of Biological Chemistry, 2003
- Apocytochrome c Blocks Caspase-9 Activation and Bax-induced ApoptosisJournal of Biological Chemistry, 2002
- Neuroglobin and cytoglobinEMBO Reports, 2002
- A modeling study of the interaction and electron transfer between cytochrome b 5 and some oxidized haemoglobinsJBIC Journal of Biological Inorganic Chemistry, 2001
- Analysis of redox regulation of cytochrome c-induced apoptosis in a cell-free systemCell Death & Differentiation, 1999
- Induction of Apoptotic Program in Cell-Free Extracts: Requirement for dATP and Cytochrome cPublished by Elsevier ,1996
- Oxidation-reduction equilibrium of cytochrome b5Journal of the American Chemical Society, 1982
- Spectra of cytochrome c monomer and polymersBiochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects, 1963