Hydrogen bonding of iron-coordinated histidine in heme proteins.
The hydrogen-bonding motifs of the proton on the N delta atom of iron-coordinated histidine residues in heme proteins have been classified into three categories: (1) Those in which the hydrogen-bond acceptor is either an amino acid residue (serine) directly adjacent to the histidine or a carbonyl group of the polypeptide chain less than five residues away from the histidine; (2) those in which the hydrogen-bonding acceptor is a carbonyl group of the polypeptide backbone associated with an amino acid residue 8 to 17 residues away from the histidine; and (3) those in which the hydrogen-bonding acceptor is an exogenous water molecule or an amino acid residue located far from the histidine in the amino acid sequence. Some biological functions are defined by this classification, whereas others span all classes.
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AT&T Bell Laboratories, Murray Hill, New Jersey 07974.
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D000818:Animals; D001426:Bacterial Proteins / Q000737:chemistry; D003580:Cytochromes / Q000737:chemistry; D006420:Hemeproteins / Q000737:chemistry*; D006639:Histidine / Q000737:chemistry*; D006860:Hydrogen Bonding; D007501:Iron / Q000737:chemistry*; D010084:Oxidation-Reduction; D014961:X-Ray Diffraction
D001426:Bacterial Proteins; D003580:Cytochromes; D006420:Hemeproteins; D006639:Histidine; D007501:Iron