@article {488,
	title = {Role of the distal hydrogen-bonding network in regulating oxygen affinity in the truncated hemoglobin III from Campylobacter jejuni},
	journal = {Biochemistry},
	volume = {50},
	year = {2011},
	month = {2011/05/17/},
	pages = {3946 - 3956},
	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.},
	keywords = {Bacterial Proteins/chemistry/genetics; Campylobacter jejuni/chemistry/genetics; Glycine/genetics; Heme/chemistry/genetics; Histidine/chemistry/genetics; Hydrogen Bonding; Ligands; Molecular Dynamics Simulation; Mutagenesis, Raman; Truncated Hemoglobins/chemistry/genetics; Tryptophan/chemistry/genetics; Tyrosine/chemistry/genetics, Site-Directed; Oxygen/chemistry/metabolism; Protein Binding/genetics; Spectrum Analysis},
	author = {Manez,P. Arroyo and Lu,C. and Boechi,L. and M. A. Marti and Shepherd,M. and Wilson,J. L. and Poole,R. K. and F. J. Luque and Yeh,S. R. and D. A. Estrin}
}
