A light-dependent complementation system for analysis of NADPH:protochlorophyllide oxidoreductase: identification and mutagenesis of two conserved residues that are essential for enzyme activity.
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Chlorophyll BiosynthesisEvolutionary Aspects and Regulation of Tetrapyrrole Biosynthesis in Cyanobacteria under Aerobic and Anaerobic EnvironmentsProtochlorophyllide oxidoreductase B-catalyzed protochlorophyllide photoreduction in vitro: insight into the mechanism of chlorophyll formation in light-adapted plantsUltrafast enzymatic reaction dynamics in protochlorophyllide oxidoreductase.Laser excitation studies of the product release steps in the catalytic cycle of the light-driven enzyme, protochlorophyllide oxidoreductase.Cryogenic and laser photoexcitation studies identify multiple roles for active site residues in the light-driven enzyme protochlorophyllide oxidoreductaseDark-operative protochlorophyllide oxidoreductase generates substrate radicals by an iron-sulphur cluster in bacteriochlorophyll biosynthesis.Enzymology below 200 K: the kinetics and thermodynamics of the photochemistry catalyzed by protochlorophyllide oxidoreductaseExtensive horizontal gene transfer, duplication, and loss of chlorophyll synthesis genes in the algaeDifferential Regulation of Duplicate Light-Dependent Protochlorophyllide Oxidoreductases in the Diatom Phaeodactylum tricornutum.Photoprotective role of NADPH:protochlorophyllide oxidoreductase A.Excited state dynamics and catalytic mechanism of the light-driven enzyme protochlorophyllide oxidoreductase.Purification and kinetic analysis of pea (Pisum sativum L.) NADPH:protochlorophyllide oxidoreductase expressed as a fusion with maltose-binding protein in Escherichia coli.Three classes of oxygen-dependent cyclase involved in chlorophyll and bacteriochlorophyll biosynthesis.NADPH:protochlorophyllide oxidoreductase B (PORB) action in Arabidopsis thaliana revisited through transgenic expression of engineered barley PORB mutant proteins.Secondary structure of NADPH: protochlorophyllide oxidoreductase examined by circular dichroism and prediction methods.Plant Protochlorophyllide Oxidoreductases A and B: CATALYTIC EFFICIENCY AND INITIAL REACTION STEPS.Excited-state dynamics of protochlorophyllide revealed by subpicosecond infrared spectroscopy.Spectroscopic and kinetic characterization of the light-dependent enzyme protochlorophyllide oxidoreductase (POR) using monovinyl and divinyl substrates.Mutation of tyrosine-194 and lysine-198 in the catalytic site of pig 3alpha/beta,20beta-hydroxysteroid dehydrogenase.With or without light: comparing the reaction mechanism of dark-operative protochlorophyllide oxidoreductase with the energetic requirements of the light-dependent protochlorophyllide oxidoreductase.Protochlorophyllide oxidoreductase: a homology model examined by site-directed mutagenesis.The importance of the C-terminal region and Cys residues for the membrane association of the NADPH:protochlorophyllide oxidoreductase in pea.Association of the NADPH:protochlorophyllide oxidoreductase (POR) with isolated etioplast inner membranes from wheat.The effects of low pH on the properties of protochlorophyllide oxidoreductase and the organization of prolamellar bodies of maize (Zea mays).The extra loop distinguishing POR from the structurally related short-chain alcohol dehydrogenases is dispensable for pigment binding but needed for the assembly of light-harvesting POR-protochlorophyllide complex.Wavelength-dependent photooxidation and photoreduction of protochlorophyllide and protochlorophyll in the innermost leaves of cabbage (Brassica oleracea var. capitata L.).Identification and light-induced expression of a novel gene of NADPH-protochlorophyllide oxidoreductase isoform in Arabidopsis thaliana.Stepwise Hydride Transfer in a Biological System: Insights into the Reaction Mechanism of the Light-Dependent Protochlorophyllide Oxidoreductase.Enzyme activation and catalysis: characterisation of the vibrational modes of substrate and product in protochlorophyllide oxidoreductase.Origin and evolution of the light-dependent protochlorophyllide oxidoreductase (LPOR) genes.Computational insights into the photochemical step of the reaction catalyzed by protochlorophylide oxidoreductase
P2860
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P2860
A light-dependent complementation system for analysis of NADPH:protochlorophyllide oxidoreductase: identification and mutagenesis of two conserved residues that are essential for enzyme activity.
description
1995 nî lūn-bûn
@nan
1995 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
A light-dependent complementat ...... essential for enzyme activity.
@ast
A light-dependent complementat ...... essential for enzyme activity.
@en
type
label
A light-dependent complementat ...... essential for enzyme activity.
@ast
A light-dependent complementat ...... essential for enzyme activity.
@en
prefLabel
A light-dependent complementat ...... essential for enzyme activity.
@ast
A light-dependent complementat ...... essential for enzyme activity.
@en
P2860
P356
P1476
A light-dependent complementat ...... essential for enzyme activity.
@en
P2093
P2860
P304
P356
10.1073/PNAS.92.3.724
P407
P577
1995-01-01T00:00:00Z