DiazeneA Not so Innocent Ligand for the Binuclear Center of Cytochrome c Oxidase
- 16 October 1998
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 37 (44) , 15583-15592
- https://doi.org/10.1021/bi981476m
Abstract
Diazene reacts rapidly with cytochrome c oxidase to reduce cytochrome a and CuA and to form a charge-transfer complex with ferric cytochrome a3; the diazene may serve to bridge the heme iron of this cytochrome and CuB. The complex is characterized by an intense, optically active absorbance located at 847 nm. A similar band had been observed previously upon reduction of cytochrome oxidase with hydrazine [Markossian, K. A., Paitian, N. A., and Nalbandyan, R. M. (1983) FEBS Lett. 156, 235−238], but it appears that this band is actually due to the diazene produced as a result of the oxidation of the hydrazine that occurs in this process. A similar diazene to iron charge-transfer band is found following the reaction of diazene with ferric horseradish peroxidase and with hemin chloride but not with met-myoglobin.Keywords
This publication has 5 references indexed in Scilit:
- Activation of Diazene and the Nitrogenase Problem: An Investigation of Diazene-Bridged Fe(II) Centers with Sulfur Ligand Sphere. 1. Electronic StructureJournal of the American Chemical Society, 1997
- Hydrazine and hydroxylamine as probes for O2-reduction site of mitochondrial cytochrome c oxidaseBiochemical Journal, 1993
- Formation and reduction of a ‘peroxy’ intermediate of cytochrome c oxidase by hydrogen peroxideBiochemical Journal, 1984
- Changes induced by hydrazine in optical spectra of cytochrome oxidaseFEBS Letters, 1983
- Electron redistribution in cytochrome c oxidase during freezing under turnover conditionsFEBS Letters, 1981