Conformational events during ternary enzyme-substrate complex formation are rate limiting in the catalytic cycle of the light-driven enzyme protochlorophyllide oxidoreductase

Biochemistry

Volumn 47, Issue 41, 2008, Pages 10991-10998

  Heyes, Derren J ^a   Menon, Binuraj R K ^a   Sakuma, Michiyo ^a   Scrutton, Nigel S ^a  

^a UNIVERSITY OF MANCHESTER   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING SITES; BIOCHEMICAL ENGINEERING; BIOCHEMISTRY; CATALYSIS; CHLOROPHYLL; ELECTROMAGNETIC WAVES; ENZYMES; HYDROGEN; PHOTOCHEMICAL REACTIONS; PORPHYRINS; RATE CONSTANTS; REACTION KINETICS;

ACTIVE SITES; BINDING EVENTS; CATALYTIC CYCLING; CHLOROPHYLL BIOSYNTHESIS; COFACTOR; CONFORMATIONAL CHANGES; CONFORMATIONAL STATES; DOUBLE BONDS; EN-ROUTE; ENZYME-SUBSTRATE COMPLEXES; HYDROGEN-TRANSFER REACTIONS; KINETIC PROBES; MODEL SYSTEMS; PHOTOACTIVATION; PROTEIN MOTIONS; PROTOCHLOROPHYLLIDE; PROTOCHLOROPHYLLIDE OXIDOREDUCTASE; RATE-LIMITING; RATE-LIMITING STEP; REACTIVE CONFORMATION; SUBSTRATE BINDING; TERNARY COMPLEX FORMATION; TERNARY COMPLEXES;

SUBSTRATES;

OXIDOREDUCTASE; PROTOCHLOROPHYLLIDE; PROTOCHLOROPHYLLIDE OXIDOREDUCTASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; CONFORMATIONAL TRANSITION; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ENZYME CONFORMATION; ENZYME KINETICS; ENZYME SUBSTRATE COMPLEX; NONHUMAN; PRIORITY JOURNAL; THERMODYNAMICS;

CATALYSIS; FLUORESCENCE RESONANCE ENERGY TRANSFER; KINETICS; LIGHT; NADP; OXIDOREDUCTASES ACTING ON CH-CH GROUP DONORS; PROTEIN BINDING; PROTEIN CONFORMATION; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; SUBSTRATE SPECIFICITY;

EID: 53749083819     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi801521c     Document Type: Article

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