Arroyo Mañez, Pau, Lu, Changyuan, Boechi, Leonardo, Martí, Marcelo A, Shepherd, Mark, Wilson, Jayne Louise, Poole, Robert K, Luque, F Javier, Yeh, Syun-Ru, Estrin, Darío A and others. (2011) Role of the distal hydrogen-bonding network in regulating oxygen affinity in the truncated hemoglobin III from Campylobacter jejuni. Biochemistry, 50 (19). pp. 3946-3956. ISSN 1520-4995. (doi:10.1021/bi101137n) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:28107)
The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided. | |
Official URL: http://dx.doi.org/10.1021/bi101137n |
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.
Item Type: | Article |
---|---|
DOI/Identification number: | 10.1021/bi101137n |
Subjects: | Q Science |
Divisions: | Divisions > Division of Natural Sciences > Biosciences |
Depositing User: | Mark Shepherd |
Date Deposited: | 01 Sep 2011 15:47 UTC |
Last Modified: | 16 Nov 2021 10:06 UTC |
Resource URI: | https://kar.kent.ac.uk/id/eprint/28107 (The current URI for this page, for reference purposes) |
- Export to:
- RefWorks
- EPrints3 XML
- BibTeX
- CSV
- Depositors only (login required):