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Title: Redox control of fast ligand dissociation from Escherichia coli cytochrome bd

Abstract

Bacterial bd-type quinol oxidases, such as cytochrome bd from Escherichia coli, contain three hemes, but no copper. In contrast to heme-copper oxidases and similarly to globins, single electron-reduced cytochrome bd forms stable complexes with O{sub 2}, NO and CO at ferrous heme d. Kinetics of ligand dissociation from heme d {sup 2+} in the single electron- and fully-reduced cytochrome bd from E. coli has been investigated by rapid mixing spectrophotometry at 20 {sup o}C. Data show that (i) O{sub 2} dissociates at 78 s{sup -1} (ii) NO and CO dissociation is fast as compared to heme-copper oxidases and (iii) dissociation in the single electron-reduced state is hindered as compared to the fully-reduced enzyme. Presumably, rapid ligand dissociation requires reduced heme b {sub 595}. As NO, an inhibitor of respiratory oxidases, is involved in the immune response against microbial infection, the rapid dissociation of NO from cytochrome bd may have important bearings on the patho-physiology of enterobacteria.

Authors:
 [1];  [2];  [2];  [2];  [1];  [3]
  1. Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow 119992 (Russian Federation)
  2. Department of Biochemical Sciences, CNR Institute of Molecular Biology and Pathology, University of Rome 'La Sapienza', Rome I-00185 (Italy)
  3. Department of Biochemical Sciences, CNR Institute of Molecular Biology and Pathology, University of Rome 'La Sapienza', Rome I-00185 (Italy). E-mail: alessandro.giuffre@uniroma1.it
Publication Date:
OSTI Identifier:
20979857
Resource Type:
Journal Article
Resource Relation:
Journal Name: Biochemical and Biophysical Research Communications; Journal Volume: 355; Journal Issue: 1; Other Information: DOI: 10.1016/j.bbrc.2007.01.118; PII: S0006-291X(07)00167-2; Copyright (c) 2007 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; CARBON MONOXIDE; COPPER; DISSOCIATION; ELECTRONS; ESCHERICHIA COLI; HEME; LIGANDS; MYOGLOBIN; NITRIC OXIDE; OXIDASES; PHYSIOLOGY; REACTION KINETICS; RESPIRATION; SPECTROPHOTOMETRY; SPECTROSCOPY

Citation Formats

Borisov, Vitaliy B., Forte, Elena, Sarti, Paolo, Brunori, Maurizio, Konstantinov, Alexander A., and Giuffre, Alessandro. Redox control of fast ligand dissociation from Escherichia coli cytochrome bd. United States: N. p., 2007. Web. doi:10.1016/j.bbrc.2007.01.118.
Borisov, Vitaliy B., Forte, Elena, Sarti, Paolo, Brunori, Maurizio, Konstantinov, Alexander A., & Giuffre, Alessandro. Redox control of fast ligand dissociation from Escherichia coli cytochrome bd. United States. doi:10.1016/j.bbrc.2007.01.118.
Borisov, Vitaliy B., Forte, Elena, Sarti, Paolo, Brunori, Maurizio, Konstantinov, Alexander A., and Giuffre, Alessandro. Fri . "Redox control of fast ligand dissociation from Escherichia coli cytochrome bd". United States. doi:10.1016/j.bbrc.2007.01.118.
@article{osti_20979857,
title = {Redox control of fast ligand dissociation from Escherichia coli cytochrome bd},
author = {Borisov, Vitaliy B. and Forte, Elena and Sarti, Paolo and Brunori, Maurizio and Konstantinov, Alexander A. and Giuffre, Alessandro},
abstractNote = {Bacterial bd-type quinol oxidases, such as cytochrome bd from Escherichia coli, contain three hemes, but no copper. In contrast to heme-copper oxidases and similarly to globins, single electron-reduced cytochrome bd forms stable complexes with O{sub 2}, NO and CO at ferrous heme d. Kinetics of ligand dissociation from heme d {sup 2+} in the single electron- and fully-reduced cytochrome bd from E. coli has been investigated by rapid mixing spectrophotometry at 20 {sup o}C. Data show that (i) O{sub 2} dissociates at 78 s{sup -1} (ii) NO and CO dissociation is fast as compared to heme-copper oxidases and (iii) dissociation in the single electron-reduced state is hindered as compared to the fully-reduced enzyme. Presumably, rapid ligand dissociation requires reduced heme b {sub 595}. As NO, an inhibitor of respiratory oxidases, is involved in the immune response against microbial infection, the rapid dissociation of NO from cytochrome bd may have important bearings on the patho-physiology of enterobacteria.},
doi = {10.1016/j.bbrc.2007.01.118},
journal = {Biochemical and Biophysical Research Communications},
number = 1,
volume = 355,
place = {United States},
year = {Fri Mar 30 00:00:00 EDT 2007},
month = {Fri Mar 30 00:00:00 EDT 2007}
}