Enzyme activation and catalysis: characterisation of the vibrational modes of substrate and product in protochlorophyllide oxidoreductase.

about

Excited state dynamics and catalytic mechanism of the light-driven enzyme protochlorophyllide oxidoreductase.

P2860

Q37993782-CCBD4459-D26A-46B9-B855-6655FADC2228

P2860

Enzyme activation and catalysis: characterisation of the vibrational modes of substrate and product in protochlorophyllide oxidoreductase.

Item

http://www.wikidata.org/entity/Q50554059

description

2010 nî lūn-bûn

@nan

2010年の論文

@ja

2010年学术文章

@wuu

2010年学术文章

@zh

2010年学术文章

@zh-cn

2010年学术文章

@zh-hans

2010年学术文章

@zh-my

2010年学术文章

@zh-sg

2010年學術文章

@yue

2010年學術文章

@zh-hant

name

Enzyme activation and catalysi ...... chlorophyllide oxidoreductase.

@en

Enzyme activation and catalysi ...... chlorophyllide oxidoreductase.

@nl

type

Item

label

Enzyme activation and catalysi ...... chlorophyllide oxidoreductase.

@en

Enzyme activation and catalysi ...... chlorophyllide oxidoreductase.

@nl

prefLabel

Enzyme activation and catalysi ...... chlorophyllide oxidoreductase.

@en

Enzyme activation and catalysi ...... chlorophyllide oxidoreductase.

@nl

P1476

Enzyme activation and catalysi ...... chlorophyllide oxidoreductase.

@en

P2093

Bruno Robert

http://www.w3.org/2001/XMLSchema#string

C Neil Hunter

http://www.w3.org/2001/XMLSchema#string

Marie Louise Groot

http://www.w3.org/2001/XMLSchema#string

Maxime T Alexandre

http://www.w3.org/2001/XMLSchema#string

Olga A Sytina

http://www.w3.org/2001/XMLSchema#string

P2860

Stretched exponential decay and correlations in the catalytic activity of fluctuating single lipase molecules

Single-molecule enzymatic dynamics

A Fourier-transform infrared spectroscopic investigation of the hydrogen-deuterium exchange and secondary structure of the 28-kDa channel-forming integral membrane protein (CHIP28).

A light-dependent complementation system for analysis of NADPH:protochlorophyllide oxidoreductase: identification and mutagenesis of two conserved residues that are essential for enzyme activity.

Ultrafast 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.

Conformational changes in an ultrafast light-driven enzyme determine catalytic activity.

Cryogenic and laser photoexcitation studies identify multiple roles for active site residues in the light-driven enzyme protochlorophyllide oxidoreductase

Infrared spectroelectrochemistry of bacteriochlorophylls and bacteriopheophytins: Implications for the binding of the pigments in the reaction center from photosynthetic bacteria.

External reflection FTIR of peptide monolayer films in situ at the air/water interface: experimental design, spectra-structure correlations, and effects of hydrogen-deuterium exchange.

P304

2307-2313

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1039/C0CP01686A

http://www.w3.org/2001/XMLSchema#string

P407

English

P433

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P50

Rienk van Grondelle

Derren J Heyes

P577

2010-11-22T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

21103538

http://www.w3.org/2001/XMLSchema#string

Enzyme activation and catalysis: characterisation of the vibrational modes of substrate and product in protochlorophyllide oxidoreductase.

about

P2860

P2860

Enzyme activation and catalysis: characterisation of the vibrational modes of substrate and product in protochlorophyllide oxidoreductase.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698