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Role of the distal hydrogen-bonding network in regulating oxygen affinity in the truncated hemoglobin III from Campylobacter jejuni

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)

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. (Contact us about this Publication)
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: Faculties > Sciences > School of Biosciences
Depositing User: Mark Shepherd
Date Deposited: 01 Sep 2011 15:47 UTC
Last Modified: 23 Jan 2020 04:05 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/28107 (The current URI for this page, for reference purposes)
Shepherd, Mark: https://orcid.org/0000-0002-7472-2300
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