Hydrogen bonding of iron-coordinated histidine in heme proteins

Rousseau G. Douglas, Denis L. Rousseau

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

The hydrogen-bonding motifs of the proton on the Nδ 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.

Original languageEnglish (US)
Pages (from-to)13-17
Number of pages5
JournalJournal of Structural Biology
Volume109
Issue number1
DOIs
StatePublished - 1992
Externally publishedYes

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Hemeproteins
Hydrogen Bonding
Histidine
Iron
Amino Acids
Peptides
Serine
Protons
Hydrogen
Amino Acid Sequence
Water

ASJC Scopus subject areas

  • Structural Biology

Cite this

Hydrogen bonding of iron-coordinated histidine in heme proteins. / Douglas, Rousseau G.; Rousseau, Denis L.

In: Journal of Structural Biology, Vol. 109, No. 1, 1992, p. 13-17.

Research output: Contribution to journalArticle

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