Literature DB >> 11034350

The influence of glycerol and chloroplast lipids on the spectral shifts of pigments associated with NADPH: protochlorophyllide oxidoreductase from Avena sativa L.

H Klement1, U Oster, W Rüdiger.   

Abstract

Dark-grown angiosperm seedlings lack chlorophylls, but accumulate protochlorophyllide a complexed with the light-dependent enzyme NADPH:protochlorophyllide oxidoreductase. Previous investigators correlated spectral heterogeneity of in vivo protochlorophyllide forms and a shift of chlorophyllide forms from 680 to 672 nm (Shibata shift) occurring after irradiation, with intact membrane structures which are destroyed by solubilization. We demonstrate here that the various protochlorophyllide forms and the Shibata shift which disappear upon solubilization are restored if the reconstituted complex is treated with plastid lipids and 80% (w/v) glycerol. We hypothesize that the lipids can form a cubic phase and that this is the precondition in vitro and in vivo for the observed spectral properties before and after irradiation.

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Year:  2000        PMID: 11034350     DOI: 10.1016/s0014-5793(00)01887-1

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  7 in total

1.  NADPH:protochlorophyllide oxidoreductase B (PORB) action in Arabidopsis thaliana revisited through transgenic expression of engineered barley PORB mutant proteins.

Authors:  Frank Buhr; Abderrahim Lahroussi; Armin Springer; Sachin Rustgi; Diter von Wettstein; Christiane Reinbothe; Steffen Reinbothe
Journal:  Plant Mol Biol       Date:  2017-03-04       Impact factor: 4.076

2.  Novel Insights into the Enzymology, Regulation and Physiological Functions of Light-dependent Protochlorophyllide Oxidoreductase in Angiosperms.

Authors:  Tatsuru Masuda; Ken-Ichiro Takamiya
Journal:  Photosynth Res       Date:  2004       Impact factor: 3.573

3.  The relationship between different spectral forms of the protochlorophyllide oxidoreductase complex and the structural organisation of prolamellar bodies isolated from Zea mays.

Authors:  Eva Selstam; Anthony P R Brain; W Patrick Williams
Journal:  Photosynth Res       Date:  2011-04-20       Impact factor: 3.573

4.  POR structural domains important for the enzyme activity in R. capsulatus complementation system.

Authors:  Nikolai Lebedev; Michael P Timko
Journal:  Photosynth Res       Date:  2002       Impact factor: 3.573

5.  On the nature of the two pathways in chlorophyll formation from protochlorophyllide.

Authors:  V P Domanskii; W Rüdiger
Journal:  Photosynth Res       Date:  2001       Impact factor: 3.573

6.  Enzymology below 200 K: the kinetics and thermodynamics of the photochemistry catalyzed by protochlorophyllide oxidoreductase.

Authors:  Derren J Heyes; Alexander V Ruban; Helen M Wilks; C Neil Hunter
Journal:  Proc Natl Acad Sci U S A       Date:  2002-08-12       Impact factor: 11.205

7.  Photoactive protochlorophyllide-enzyme complexes reconstituted with PORA, PORB and PORC proteins of A. thaliana: fluorescence and catalytic properties.

Authors:  Michał Gabruk; Anna Stecka; Wojciech Strzałka; Jerzy Kruk; Kazimierz Strzałka; Beata Mysliwa-Kurdziel
Journal:  PLoS One       Date:  2015-02-06       Impact factor: 3.240

  7 in total

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