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The carboxin-binding site on Paracoccus denitrificans succinate:quinone reductase identified by mutation and structure comparison

Matsson, Mikael and Hederstedt, Lars LU (2001) In Journal of Bioenergetics and Biomembranes 33. p.99-105
Abstract
Succinate:quinone reductase catalyzes electron transfer from succinate to quinone in aerobic respiration. Carboxin is a specific inhibitor of this enzyme from several different organisms. We have isolated mutant strains of the bacterium Paracoccus denitrificans that are resistant to carboxin due to mutations in the succinate:quinone reductase. The mutations identify two amino acid residues, His228 in SdhB and Asp89 in SdhD, that most likely constitute part of a carboxin-binding site. This site is in the same region of the enzyme as the proposed active site for ubiquinone reduction. From the combined mutant data and structural information derived from Escherichia coli and Wolinella succinogenes quinol:fumarate reductase, we suggest that... (More)
Succinate:quinone reductase catalyzes electron transfer from succinate to quinone in aerobic respiration. Carboxin is a specific inhibitor of this enzyme from several different organisms. We have isolated mutant strains of the bacterium Paracoccus denitrificans that are resistant to carboxin due to mutations in the succinate:quinone reductase. The mutations identify two amino acid residues, His228 in SdhB and Asp89 in SdhD, that most likely constitute part of a carboxin-binding site. This site is in the same region of the enzyme as the proposed active site for ubiquinone reduction. From the combined mutant data and structural information derived from Escherichia coli and Wolinella succinogenes quinol:fumarate reductase, we suggest that carboxin acts by blocking binding of ubiquinone to the active site. The block would be either by direct exclusion of uhiquinone from the active site or by occlusion of a pore that leads to the active site. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
succinate dehydrogenase, carboxin, TTFA, ubiquinone
in
Journal of Bioenergetics and Biomembranes
volume
33
pages
99 - 105
publisher
Kluwer
external identifiers
  • scopus:0035005674
ISSN
1573-6881
DOI
10.1023/A:1010744330092
language
English
LU publication?
yes
id
ec52fb12-35b2-489e-ba51-48ae956a4d44
date added to LUP
2017-07-17 11:54:08
date last changed
2018-05-29 11:09:46
@article{ec52fb12-35b2-489e-ba51-48ae956a4d44,
  abstract     = {Succinate:quinone reductase catalyzes electron transfer from succinate to quinone in aerobic respiration. Carboxin is a specific inhibitor of this enzyme from several different organisms. We have isolated mutant strains of the bacterium Paracoccus denitrificans that are resistant to carboxin due to mutations in the succinate:quinone reductase. The mutations identify two amino acid residues, His228 in SdhB and Asp89 in SdhD, that most likely constitute part of a carboxin-binding site. This site is in the same region of the enzyme as the proposed active site for ubiquinone reduction. From the combined mutant data and structural information derived from Escherichia coli and Wolinella succinogenes quinol:fumarate reductase, we suggest that carboxin acts by blocking binding of ubiquinone to the active site. The block would be either by direct exclusion of uhiquinone from the active site or by occlusion of a pore that leads to the active site.},
  author       = {Matsson, Mikael and Hederstedt, Lars},
  issn         = {1573-6881},
  keyword      = {succinate dehydrogenase,carboxin,TTFA,ubiquinone},
  language     = {eng},
  pages        = {99--105},
  publisher    = {Kluwer},
  series       = {Journal of Bioenergetics and Biomembranes},
  title        = {The carboxin-binding site on <em>Paracoccus denitrificans</em> succinate:quinone reductase identified by mutation and structure comparison},
  url          = {http://dx.doi.org/10.1023/A:1010744330092},
  volume       = {33},
  year         = {2001},
}