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The reaction of neuroglobin with potential redox protein partners cytochrome b 5 and cytochrome c
Author(s) -
Fago Angela,
Mathews Antony J.,
Moens Luc,
Dewilde Sylvia,
Brittain Thomas
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.08.003
Subject(s) - neuroglobin , redox , cytochrome , cytochrome c , chemistry , cytochrome b , biochemistry , globin , hemoglobin , mitochondrion , gene , enzyme , inorganic chemistry , mitochondrial dna
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 × 10 2 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 × 10 7 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.