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

Pau Arroyo Mañez, Changyuan Lu, Leonardo Boechi, Marcelo A. Martí, Mark Shepherd, Jayne Louise Wilson, Robert K. Poole, F. Javier Luque, Syun-Ru Yeh, Darío A. Estrin

Research output: Contribution to journalArticle

18 Citations (Scopus)

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 G8WF mutant of Ctb and employed state-of-the-art computer simulation methods to investigate the properties of the O2 adduct of the G8 WF mutant, with respect to those of the wild-type protein and the previously studied E7HL and/or B10YF 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.

Original languageEnglish (US)
Pages (from-to)3946-3956
Number of pages11
JournalBiochemistry
Volume50
Issue number19
DOIs
StatePublished - May 17 2011

Fingerprint

Truncated Hemoglobins
Campylobacter jejuni
Hydrogen Bonding
Hydrogen bonds
Heme
Oxygen
Computer Simulation
Conformations
Hydrogen
Proteins
Ligands
Kinetics
Computer simulation

ASJC Scopus subject areas

  • Biochemistry

Cite this

Arroyo Mañez, P., Lu, C., Boechi, L., Martí, M. A., Shepherd, M., Wilson, J. L., ... Estrin, D. A. (2011). Role of the distal hydrogen-bonding network in regulating oxygen affinity in the truncated hemoglobin III from campylobacter jejuni. Biochemistry, 50(19), 3946-3956. https://doi.org/10.1021/bi101137n

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.

In: Biochemistry, Vol. 50, No. 19, 17.05.2011, p. 3946-3956.

Research output: Contribution to journalArticle

Arroyo Mañez, P, Lu, C, Boechi, L, Martí, MA, Shepherd, M, Wilson, JL, Poole, RK, Luque, FJ, Yeh, S-R & Estrin, DA 2011, 'Role of the distal hydrogen-bonding network in regulating oxygen affinity in the truncated hemoglobin III from campylobacter jejuni', Biochemistry, vol. 50, no. 19, pp. 3946-3956. https://doi.org/10.1021/bi101137n
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. / Role of the distal hydrogen-bonding network in regulating oxygen affinity in the truncated hemoglobin III from campylobacter jejuni. In: Biochemistry. 2011 ; Vol. 50, No. 19. pp. 3946-3956.
@article{eadd31c1624645a4a9e07569fcbfc0eb,
title = "Role of the distal hydrogen-bonding network in regulating oxygen affinity in the truncated hemoglobin III from campylobacter jejuni",
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 G8WF mutant of Ctb and employed state-of-the-art computer simulation methods to investigate the properties of the O2 adduct of the G8 WF mutant, with respect to those of the wild-type protein and the previously studied E7HL and/or B10YF 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.",
author = "{Arroyo Ma{\~n}ez}, Pau and Changyuan Lu and Leonardo Boechi and Mart{\'i}, {Marcelo A.} and Mark Shepherd and Wilson, {Jayne Louise} and Poole, {Robert K.} and Luque, {F. Javier} and Syun-Ru Yeh and Estrin, {Dar{\'i}o A.}",
year = "2011",
month = "5",
day = "17",
doi = "10.1021/bi101137n",
language = "English (US)",
volume = "50",
pages = "3946--3956",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "American Chemical Society",
number = "19",

}

TY - JOUR

T1 - Role of the distal hydrogen-bonding network in regulating oxygen affinity in the truncated hemoglobin III from campylobacter jejuni

AU - Arroyo Mañez, Pau

AU - Lu, Changyuan

AU - Boechi, Leonardo

AU - Martí, Marcelo A.

AU - Shepherd, Mark

AU - Wilson, Jayne Louise

AU - Poole, Robert K.

AU - Luque, F. Javier

AU - Yeh, Syun-Ru

AU - Estrin, Darío A.

PY - 2011/5/17

Y1 - 2011/5/17

N2 - 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 G8WF mutant of Ctb and employed state-of-the-art computer simulation methods to investigate the properties of the O2 adduct of the G8 WF mutant, with respect to those of the wild-type protein and the previously studied E7HL and/or B10YF 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.

AB - 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 G8WF mutant of Ctb and employed state-of-the-art computer simulation methods to investigate the properties of the O2 adduct of the G8 WF mutant, with respect to those of the wild-type protein and the previously studied E7HL and/or B10YF 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.

UR - http://www.scopus.com/inward/record.url?scp=79955825038&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=79955825038&partnerID=8YFLogxK

U2 - 10.1021/bi101137n

DO - 10.1021/bi101137n

M3 - Article

C2 - 21476539

AN - SCOPUS:79955825038

VL - 50

SP - 3946

EP - 3956

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 19

ER -