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Volumn 40, Issue 42, 2001, Pages 12562-12574
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Tyr275 and Lys279 stabilize NADPH within the catalytic site of NADPH:protochlorophyllide oxidoreductase and are involved in the formation of the enzyme photoactive state
a
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Author keywords
[No Author keywords available]
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Indexed keywords
HYDROGEN TRANSFER;
AMINO ACIDS;
CATALYSIS;
ESCHERICHIA COLI;
FLUORESCENCE;
PHOTOCHEMICAL REACTIONS;
SPECTROSCOPY;
ENZYMES;
AMINO ACID;
ARGININE;
CHLOROPHYLLIDE;
HYDROGEN;
ISOLEUCINE;
LYSINE;
PHENYLALANINE;
PROTOCHLOROPHYLLIDE;
REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;
REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE DEHYDROGENASE;
TYROSINE;
ARTICLE;
CONTROLLED STUDY;
ENZYME ACTIVE SITE;
ENZYME ACTIVITY;
ENZYME DENATURATION;
ENZYME KINETICS;
ENZYME STRUCTURE;
ENZYME SUBSTRATE COMPLEX;
ESCHERICHIA COLI;
NONHUMAN;
PEA;
PHOTOACTIVATION;
PHOTOCHEMISTRY;
PRIORITY JOURNAL;
PROTON TRANSPORT;
SITE DIRECTED MUTAGENESIS;
SPECTROFLUOROMETRY;
STEREOISOMERISM;
STRUCTURE ACTIVITY RELATION;
STRUCTURE ANALYSIS;
AMINO ACID SUBSTITUTION;
BINDING SITES;
CATALYTIC DOMAIN;
ENZYME ACTIVATION;
ENZYME STABILITY;
FREEZING;
KINETICS;
LYSINE;
MUTAGENESIS, SITE-DIRECTED;
NADP;
OXIDOREDUCTASES;
OXIDOREDUCTASES ACTING ON CH-CH GROUP DONORS;
PEAS;
PHOTOCHEMISTRY;
PROTEIN DENATURATION;
PROTOCHLOROPHYLLIDE;
RHODOBACTER CAPSULATUS;
SPECTROMETRY, FLUORESCENCE;
SUBSTRATE SPECIFICITY;
TEMPERATURE;
TYROSINE;
ESCHERICHIA COLI;
PISUM SATIVUM;
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EID: 0035940442
PISSN: 00062960
EISSN: None
Source Type: Journal
DOI: 10.1021/bi0105025 Document Type: Article |
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Times cited : (49)
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References (44)
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