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NADPH-dependent thioredoxin reductase and 2-Cys peroxiredoxins are needed for the protection of Mg–protoporphyrin monomethyl ester cyclase

Stenbaek, Anne ; Hansson, Andreas LU ; Peterson Wulff, Ragna LU ; Hansson, Mats LU ; Dietz, Karl-Josef and Jensen, Poul Erik (2008) In FEBS Letters 582(18). p.2773-2778
Abstract
Abstract The chloroplast-localized NADPH-dependent thioredoxin

reductase (NTRC) has been found to be able to reduce

hydrogen peroxide scavenging 2-Cys peroxiredoxins. We show

that the Arabidopsis ntrc mutant is perturbed in chlorophyll biosynthesis

and accumulate intermediates preceding protochlorophyllide

formation. A specific involvement of NTRC during

biosynthesis of protochlorophyllide is indicated from in vitro aerobic

cyclase assays in which the conversion of Mg–protoporhyrin

monomethyl ester into protochlorophyllide is stimulated by addition

of the NTRC/2-Cys peroxiredoxin system. These findings

support the hypothesis that this NADPH-dependent... (More)
Abstract The chloroplast-localized NADPH-dependent thioredoxin

reductase (NTRC) has been found to be able to reduce

hydrogen peroxide scavenging 2-Cys peroxiredoxins. We show

that the Arabidopsis ntrc mutant is perturbed in chlorophyll biosynthesis

and accumulate intermediates preceding protochlorophyllide

formation. A specific involvement of NTRC during

biosynthesis of protochlorophyllide is indicated from in vitro aerobic

cyclase assays in which the conversion of Mg–protoporhyrin

monomethyl ester into protochlorophyllide is stimulated by addition

of the NTRC/2-Cys peroxiredoxin system. These findings

support the hypothesis that this NADPH-dependent hydrogen

peroxide scavenging system is particularly important during

periods with limited reducing power from photosynthesis, e.g. under

chloroplast biogenesis. (Less)
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author
; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Gene co-expression, Chloroplast biogenesis, Biosynthetic pathway, Hydrogen peroxide scavenging, Arabidopsis thaliana, Aerobic cyclase
in
FEBS Letters
volume
582
issue
18
pages
2773 - 2778
publisher
Wiley-Blackwell
external identifiers
  • wos:000258108400016
  • scopus:47849127156
  • pmid:18625226
ISSN
1873-3468
DOI
10.1016/j.febslet.2008.07.006
language
English
LU publication?
yes
id
93b5d11f-e984-4d5d-b1fb-0c1f6937cb3d (old id 1259763)
date added to LUP
2016-04-01 12:51:40
date last changed
2022-03-29 03:46:57
@article{93b5d11f-e984-4d5d-b1fb-0c1f6937cb3d,
  abstract     = {{Abstract The chloroplast-localized NADPH-dependent thioredoxin<br/><br>
reductase (NTRC) has been found to be able to reduce<br/><br>
hydrogen peroxide scavenging 2-Cys peroxiredoxins. We show<br/><br>
that the Arabidopsis ntrc mutant is perturbed in chlorophyll biosynthesis<br/><br>
and accumulate intermediates preceding protochlorophyllide<br/><br>
formation. A specific involvement of NTRC during<br/><br>
biosynthesis of protochlorophyllide is indicated from in vitro aerobic<br/><br>
cyclase assays in which the conversion of Mg–protoporhyrin<br/><br>
monomethyl ester into protochlorophyllide is stimulated by addition<br/><br>
of the NTRC/2-Cys peroxiredoxin system. These findings<br/><br>
support the hypothesis that this NADPH-dependent hydrogen<br/><br>
peroxide scavenging system is particularly important during<br/><br>
periods with limited reducing power from photosynthesis, e.g. under<br/><br>
chloroplast biogenesis.}},
  author       = {{Stenbaek, Anne and Hansson, Andreas and Peterson Wulff, Ragna and Hansson, Mats and Dietz, Karl-Josef and Jensen, Poul Erik}},
  issn         = {{1873-3468}},
  keywords     = {{Gene co-expression; Chloroplast
biogenesis; Biosynthetic pathway; Hydrogen peroxide
scavenging; Arabidopsis thaliana; Aerobic cyclase}},
  language     = {{eng}},
  number       = {{18}},
  pages        = {{2773--2778}},
  publisher    = {{Wiley-Blackwell}},
  series       = {{FEBS Letters}},
  title        = {{NADPH-dependent thioredoxin reductase and 2-Cys peroxiredoxins are needed for the protection of Mg–protoporphyrin monomethyl ester cyclase}},
  url          = {{http://dx.doi.org/10.1016/j.febslet.2008.07.006}},
  doi          = {{10.1016/j.febslet.2008.07.006}},
  volume       = {{582}},
  year         = {{2008}},
}