Ambidentate H-bonding of NO and O2 in heme proteins
Author:
Publisher
Elsevier BV
Subject
Inorganic Chemistry,Biochemistry
Reference64 articles.
1. Myoglobin discriminates between O2, NO, and CO by electrostatic interactions with the bound ligand
2. Mechanisms of Ligand Recognition in Myoglobin
3. A conserved residue of cytochrome P-450 is involved in heme-oxygen stability and activation
4. Uncoupling of the cytochrome P-450cam monooxygenase reaction by a single mutation, threonine-252 to alanine or valine: possible role of the hydroxy amino acid in oxygen activation.
5. Ambidentate H-bonding by heme-bound NO: structural and spectral effects of –O versus –N H-bonding
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