Hydrogen bonding interaction of the amide group of Asn and Gln at distal E7 of bovine myoglobin with bound-ligand and its functional consequences.

doi:10.1016/s0167-4838(99)00125-9

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Article

Hydrogen bonding interaction of the amide group of Asn and Gln at distal E7 of bovine myoglobin with bound-ligand and its functional consequences.

Biochimica et biophysica acta - 17 Aug 1999

Yamamoto Y, Kurihara N, Egawa T, Shimada H, Ishimura Y

Abstract excerpt

Asn and Gln with an amide group at gamma- and delta-positions, respectively, were substituted for distal His-E7 of bovine myoglobin to establish a system where hydrogen bonding interaction between the distal residue and bound-ligand can be altered by changing donor-acceptor distance. Two mutant myoglobins showed nearly identical (1)H-NMR spectral pattern for resolved heme peripheral side-chain and amino acid...

Topics

Amides
Animals
Asparagine
Base Sequence
Binding Sites
Cattle
Cyanides
Glycine
Hydrogen Bonding
Hydrogen-Ion Concentration
Kinetics

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Magnetic Resonance Spectroscopy

Metmyoglobin

Molecular Sequence Data

Mutation

Myoglobin

Oxygen

Protons

Source

Open in PubMed

Identifiers

PMID: 10446357
DOI: 10.1016/s0167-4838(99)00125-9

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-10446357-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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