The reaction of neuroglobin with potential redox protein partners cytochrome b5 and cytochrome c.
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 x 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 x 10(7)M(-1)s(-1)) with an apparent overall equilibrium constant of 1 microM. Based on this data we propose that ferrous neuroglobin may well play a role in preventing apoptosis.
Fago
Angela
A
Department of Biological Sciences, C. F. Møllers Alle 1131, Aarhus University, DK-8000 Aarhus C, Denmark.
Mathews
Antony J
AJ
Moens
Luc
L
Dewilde
Sylvia
S
Brittain
Thomas
T
D000818:Animals; D002417:Cattle; D015786:Cytochromes b5 / Q000737:chemistry*; D045304:Cytochromes c / Q000737:chemistry*; D005914:Globins / Q000737:chemistry*; D007501:Iron / Q000737:chemistry*; D051379:Mice; D009419:Nerve Tissue Proteins / Q000737:chemistry*; D000078787:Neuroglobin; D010084:Oxidation-Reduction
D009419:Nerve Tissue Proteins; D000078787:Neuroglobin; D005914:Globins; D045304:Cytochromes c; D015786:Cytochromes b5; D007501:Iron