ArticleBiochemistry2011
Role of the distal hydrogen-bonding network in regulating oxygen affinity in the truncated hemoglobin III from Campylobacter jejuni.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Intramolecular Hydrogen Bonding Enhances Stability and Reactivity of Mononuclear Cupric Superoxide Complexes.Journal of the American Chemical Society · 2018Article
- Evolutionary and Functional Relationships in the Truncated Hemoglobin Family.PLoS computational biology · 2016Article
- Electronic structure and ligand vibrations in FeNO, CoNO, and FeOO porphyrin adducts.Inorganic chemistry · 2013Article
- Gasotransmitters, poisons, and antimicrobials: it's a gas, gas, gas!F1000prime reports · 2013Article
- Ambidentate H-bonding of NO and O2 in heme proteins.Journal of inorganic biochemistry · 2012Review
Corrections and comments
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Authors and funding
10 authors.
Funding
Abstract
Oxygen affinity in heme-containing proteins is determined by a number of factors, such as the nature and conformation of the distal residues that stabilize the heme bound-oxygen via hydrogen-bonding interactions. The truncated hemoglobin III from Campylobacter jejuni (Ctb) contains three potential hydrogen-bond donors in the distal site: TyrB10, TrpG8, and HisE7. Previous studies suggested that Ctb exhibits an extremely slow oxygen dissociation rate due to an interlaced hydrogen-bonding network involving the three distal residues. Here we have studied the structural and kinetic properties of the G8(WF) mutant of Ctb and employed state-of-the-art computer simulation methods to investigate the properties of the O(2) adduct of the G8(WF) mutant, with respect to those of the wild-type protein and the previously studied E7(HL) and/or B10(YF) mutants. Our data indicate that the unique oxygen binding properties of Ctb are determined by the interplay of hydrogen-bonding interactions between the heme-bound ligand and the surrounding TyrB10, TrpG8, and HisE7 residues.
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