pH dependence of carbon monoxide binding to ferrous horseradish peroxidase.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference16 articles.
1. On the mechanism of compound I formation from peroxidases and catalases
2. Cyanide compounds of ferroperoxidase and myoglobin and their reversible photodissociation
3. Studies on the Equilibria and Kinetics of the Reactions of Peroxidases with Ligands. I. The Reaction of Ferroperoxidases with Carbon Monoxide*
4. Studies on the Equilibria and Kinetics of the Reactions of Peroxidases with Ligands. III. The Dissociation of Carbon Monoxide from Carbon Monoxide Ferro-Horseradish Peroxidase*
5. Effects of 2,4-substituents of deuteroheme upon peroxidase functions
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1. Investigations of Ferric Heme Cyanide Photodissociation in Myoglobin and Horseradish Peroxidase;The Journal of Physical Chemistry B;2013-04-03
2. A “Sliding Scale Rule” for Selectivity among NO, CO, and O2 by Heme Protein Sensors;Biochemistry;2011-12-13
3. Fluoride as a Probe for H-Bonding Interactions in the Active Site of Heme Proteins: The Case of Thermobifida fusca Hemoglobin;Journal of the American Chemical Society;2011-12-05
4. CO Binding and Ligand Discrimination in Human Myeloperoxidase;Biochemistry;2010-02-17
5. Time-resolved FTIR study of CO recombination with horseradish peroxidase;Biochemical Society Transactions;2008-11-19
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