期刊
BIOCHEMISTRY
卷 50, 期 19, 页码 3946-3956出版社
AMER CHEMICAL SOC
DOI: 10.1021/bi101137n
关键词
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资金
- Spanish Ministerio de Ciencia e Innovacion [SAF2008-05595, PCI2006-A7-0688]
- Agencia Nacional de Promocion Cientifica y Tecnologica [PICT06-25667, PME-2006-01581]
- CONICET, Universidad de Buenos Aires
- John Simon Guggenheim Foundation
- European Union
- UK Biotechnology and Biological Sciences Research Council (BBSRC) [BB/EO10504/1]
- National Science Foundation [0956358]
- BBSRC [BB/E010504/1] Funding Source: UKRI
- Division Of Chemistry
- Direct For Mathematical & Physical Scien [0956358] Funding Source: National Science Foundation
- Biotechnology and Biological Sciences Research Council [BB/E010504/1] Funding Source: researchfish
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 HI 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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