Issue 2, 1992

Iron–histidine bonding interaction in deoxymyoglobin and deoxyhaemoglobin

Abstract

Natural abundance 13C NMR resonances of the proximal histidyl imidazole carbons in the deoxy form of O2-binding haemoproteins have been observed and these resonances are found to serve as sensitive probes for the electonic stucture of this ubiquitous histidine, which is thought to control the iron reactivity.

Article information

Article type
Paper

J. Chem. Soc., Chem. Commun., 1992, 87-89

Iron–histidine bonding interaction in deoxymyoglobin and deoxyhaemoglobin

Y. Yamamoto and R. Chûjô, J. Chem. Soc., Chem. Commun., 1992, 87 DOI: 10.1039/C39920000087

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