Role of mixed oxidation states in the oxidation of hemerythrin species by ferricyanide ion
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00559a003
Reference26 articles.
1. Studies on the Oxidation-Reduction Potentials of Heme Proteins. IV. The Kinetics of Oxidation of Hemoglobin and Myoglobin by Ferricyanide*
2. Kinetics of Electron Transfer between Azurin and Cytochrome 551 from Pseudomonas
3. Preparation, disproportionation, and reactions of two semi-met forms of hemerythrin
4. The properties of hemerythrin
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2. Crystal engineering and magnetic properties of a 2D cyano-bridged NiIIFeII network formed through reduction of ferricyanide;Polyhedron;2006-06
3. Chemical and spectroscopic studies of the mixed-valent derivatives of the non-heme iron protein hemerythrin;Journal of the American Chemical Society;1991-11
4. Spectroscopic studies of the mixed-valent [iron(II), iron(III)] forms of the non-heme iron protein hemerythrin: iron coordination differences related to reactivity;Journal of the American Chemical Society;1990-02
5. Spectroscopic studies of the coupled binuclear ferric active site in methemerythrins and oxyhemerythrin: the electronic structure of each iron center and the iron-oxo and iron-peroxide bonds;Journal of the American Chemical Society;1989-06
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