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Cytochrome bd from Escherichia coli catalyzes peroxynitrite decomposition (Articolo in rivista)
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- Label
- Cytochrome bd from Escherichia coli catalyzes peroxynitrite decomposition (Articolo in rivista) (literal)
- Anno
- 2015-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1016/j.bbabio.2014.10.006 (literal)
- Alternative label
Borisov, Vitaliy; Forte, Elena; Siletsky, Sergey A.; Sarti, Paolo; Giuffrè, Alessandro (2015)
Cytochrome bd from Escherichia coli catalyzes peroxynitrite decomposition
in Biochimica et biophysica acta. Bioenergetics
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Borisov, Vitaliy; Forte, Elena; Siletsky, Sergey A.; Sarti, Paolo; Giuffrè, Alessandro (literal)
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- A.N. Belozersky Institute of Physico-Chemical Biology; Universita degli Studi di Roma La Sapienza (literal)
- Titolo
- Cytochrome bd from Escherichia coli catalyzes peroxynitrite decomposition (literal)
- Abstract
- Cytochrome bd is a prokaryotic respiratory quinol oxidase phylogenetically unrelated to heme-copper oxidases,
that was found to promote virulence in some bacterial pathogens. Cytochrome bd from Escherichia coli was
previously reported to contribute not only to proton motive force generation, but also to bacterial resistance to
nitric oxide (NOo) and hydrogen peroxide (H2O2). Here, we investigated the interaction of the purified enzyme
with peroxynitrite (ONOO-), another harmful reactive species produced by the host to kill invading microorganisms.
We found that addition of ONOO- to cytochrome bd in turnoverwith ascorbate and N,N,N?,N?-tetramethylp-
phenylenediamine (TMPD) causes the irreversible inhibition of a small (<=15%) protein fraction, due to the NOo
generated from ONOO- and not to ONOO- itself. Consistently, addition of ONOO- to cells of the E. coli strain
GO105/pTK1, expressing cytochrome bd as the only terminal oxidase, caused only a minor (<=5%) irreversible
inhibition of O2 consumption, without measurable release of NOo. Furthermore, by directly monitoring the
kinetics of ONOO- decomposition by stopped-flow absorption spectroscopy, it was found that the purified
E. coli cytochrome bd in turnover with O2 is able to metabolize ONOO- with an apparent turnover rate as high
as ~10 mol ONOO- (mol enzyme)-1 s-1 at 25 °C. To the best of our knowledge, this is the first time that the
kinetics of ONOO- decomposition by a terminal oxidase has been investigated. These results strongly suggest
a protective role of cytochrome bd against ONOO- damage. (literal)
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