Anomalously slow cyanide binding to Glycera dibranchiata monomer methemoglobin component II: implication for the equilibrium constant
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00421a011
Reference22 articles.
1. Heme-Linked Effect in the Reaction of Sperm Whale Ferrimyoglobin with Cyanide*
2. Isoelectric focusing purity criteria and proton NMR detectable spectroscopic heterogeneity in the major isolated monomer hemoglobins from Glycera dibranchiata
3. Differences in amino acid composition and heme electronic structure of the multiple monomeric hemoglobin components of Glycera dibranchiata
4. The kinetics of cyanide and fluoride binding by ferric horse-radish peroxidase
5. Kinetic and equilibrium studies of cyanide binding by cytochrome c peroxidase
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