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Protochlorophyllide oxidoreductase

Heyes DJ, Heathcote P, Rigby SEJ, Palacios MA, van Grondelle R, Hunter CN. The first catalytic step of the light-driven enzyme protochlorophyllide oxidoreductase proceeds via a charge transfer complex. J Biol Chem 2006 281 26847-53. [Pg.204]

Heyes DJ, Hunter CN. Making light work of enzyme catalysis protochlorophyllide oxidoreductase. Trends Biochem Sci 2005 30 642-9. [Pg.204]

The quantitative aspects of changes in various intracellular pools of NADPH protochlorophyllide oxidoreductase (POR) are important for understanding the principles of operation of the multienzyme system of chlorophyll biosynthesis which proteins are encoded by nuclear DBA and synthesized in the cytoplasm. The application of immunochemical methods /I,2/ allowed to detect loss of POR in the system of intraplastid membranes of etiolated leaves under illumination. In this work the enzyme-linked immunosorbent assay (ELISA) was employed for quantification of POR in different intracellular compartments of postetio-lated and green barley seedlings. [Pg.2705]

NADPH Protochlorophyllide Oxidoreductase in Barley (Hordeum vulgare) Seedlings 819... [Pg.3834]

Klement, H., Helfrich, M., Schoch, S., and Rudiger, W., Pigment-free NADPH protochlorophyllide oxidoreductase from Avena sativa L purification and substrate specificity, Eur.J. Biochem., 265, 862, 1999. [Pg.2364]

This enzyme [EC 1.3.1.33], also known as NADPH-pro-tochlorophyllide oxidoreductase, catalyzes the reaction of chlorophyllide a with NADP+ to produce protochloro-phyUide, having the (75, 85)-configuration, and NADPH. It catalyzes a light-dependent trans-reduction of the D-ring of protochlorophyllide. [Pg.582]


See other pages where Protochlorophyllide oxidoreductase is mentioned: [Pg.35]    [Pg.2377]    [Pg.2378]    [Pg.2378]    [Pg.2733]    [Pg.426]    [Pg.174]    [Pg.35]    [Pg.2377]    [Pg.2378]    [Pg.2378]    [Pg.2733]    [Pg.426]    [Pg.174]   
See also in sourсe #XX -- [ Pg.426 ]




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Oxidoreductase

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