Conformational changes in an ultrafast light-driven enzyme determine catalytic activity.
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Stabilization of the E* Form Turns Thrombin into an AnticoagulantEffects of macromolecular crowding on protein conformational changesMechanistic reappraisal of early stage photochemistry in the light-driven enzyme protochlorophyllide oxidoreductaseEvolutionary Aspects and Regulation of Tetrapyrrole Biosynthesis in Cyanobacteria under Aerobic and Anaerobic EnvironmentsRevealing time bunching effect in single-molecule enzyme conformational dynamics.Cryogenic and laser photoexcitation studies identify multiple roles for active site residues in the light-driven enzyme protochlorophyllide oxidoreductaseMutagenesis alters the catalytic mechanism of the light-driven enzyme protochlorophyllide oxidoreductaseDark-operative protochlorophyllide oxidoreductase generates substrate radicals by an iron-sulphur cluster in bacteriochlorophyll biosynthesis.Good vibrations in enzyme-catalysed reactions.Evidence of the E*-E equilibrium from rapid kinetics of Na+ binding to activated protein C and factor Xa.Photoinduced hydrogen-bonding dynamics.Serine proteases.First-principles design of nanomachines.Theoretical Study of the ESIPT Process for a New Natural Product Quercetin.Guidelines for tunneling in enzymes.Excited state dynamics and catalytic mechanism of the light-driven enzyme protochlorophyllide oxidoreductase.Hydrogen bonding and reactivity of water to azines in their S1 (n,π*) electronic excited states in the gas phase and in solution.NADPH:protochlorophyllide oxidoreductase B (PORB) action in Arabidopsis thaliana revisited through transgenic expression of engineered barley PORB mutant proteins.Excited-state dynamics of protochlorophyllide revealed by subpicosecond infrared spectroscopy.A twin-track approach has optimized proton and hydride transfer by dynamically coupled tunneling during the evolution of protochlorophyllide oxidoreductase.Excited-state charge separation in the photochemical mechanism of the light-driven enzyme protochlorophyllide oxidoreductase.Nicotinamide is a specific inhibitor of dark-operative protochlorophyllide oxidoreductase, a nitrogenase-like enzyme, from Rhodobacter capsulatus.Ultrafast intramolecular relaxation dynamics of Mg- and Zn-bacteriochlorophyll a.Conformational switching via an intramolecular H-bond modulates the fluorescence lifetime in a novel coumarin-imidazole conjugate.Enzyme activation and catalysis: characterisation of the vibrational modes of substrate and product in protochlorophyllide oxidoreductase.Synthetic, Switchable Enzymes.The molecular origin of high DNA-repair efficiency by photolyase.Cell growth defect factor1/chaperone-like protein of POR1 plays a role in stabilization of light-dependent protochlorophyllide oxidoreductase in Nicotiana benthamiana and Arabidopsis.
P2860
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P2860
Conformational changes in an ultrafast light-driven enzyme determine catalytic activity.
description
2008 nî lūn-bûn
@nan
2008 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Conformational changes in an ultrafast light-driven enzyme determine catalytic activity.
@ast
Conformational changes in an ultrafast light-driven enzyme determine catalytic activity.
@en
type
label
Conformational changes in an ultrafast light-driven enzyme determine catalytic activity.
@ast
Conformational changes in an ultrafast light-driven enzyme determine catalytic activity.
@en
prefLabel
Conformational changes in an ultrafast light-driven enzyme determine catalytic activity.
@ast
Conformational changes in an ultrafast light-driven enzyme determine catalytic activity.
@en
P2093
P356
P1433
P1476
Conformational changes in an ultrafast light-driven enzyme determine catalytic activity.
@en
P2093
C Neil Hunter
Ivo H M van Stokkum
Marie Louise Groot
Maxime T Alexandre
Olga A Sytina
P2888
P304
P356
10.1038/NATURE07354
P407
P577
2008-12-01T00:00:00Z
P5875
P6179
1025947786