A closer look at the spectroscopic properties of possible reaction intermediates in wild-type and mutant (E)-4-hydroxy-3-methylbut-2-enyl diphosphate reductase

Biochemistry

Volumn 51, Issue 24, 2012, Pages 4835-4849

  Xu, Weiya ^a   Lees, Nicholas S ^b   Hall, Dominique ^a   Welideniya, Dhanushi ^a   Hoffman, Brian M ^b   Duin, Evert C ^a  

^a AUBURN UNIVERSITY   (United States)

^b NORTHWESTERN UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AQUIFEX AEOLICUS; CATALYTIC EFFICIENCIES; CHEMICAL EQUATIONS; CLUSTER PROPERTY; DIFFERENT EFFECTS; DIPHOSPHATES; ELECTRON PARAMAGNETIC RESONANCE SPECTROSCOPY; EPR SIGNALS; HYDROXYL GROUPS; INTERMEDIATE COMPLEX; ISOPENTENYL DIPHOSPHATE; REACTION MECHANISM; REDUCTIVE ELIMINATION; SPECTROSCOPIC PROPERTY; SUBSTRATE BINDING; SUBSTRATE BINDS; SYNTHASES; TWO-PRODUCT; WILD TYPES;

EFFICIENCY; ENZYMES; MAGNETIC RESONANCE; PARAMAGNETISM; REACTION INTERMEDIATES; SUBSTRATES;

ELECTRON SPIN RESONANCE SPECTROSCOPY;

4 HYDROXY 3 METHYLBUT 2 ENYL DIPHOSPHATE REDUCTASE; FERREDOXIN; FERROUS SULFIDE; HYDROXYL GROUP; ISOPENTENYL DIPHOSPHATE; MUTANT PROTEIN; OXIDOREDUCTASE; PYROPHOSPHATE; RADICAL; THIOREDOXIN REDUCTASE; UNCLASSIFIED DRUG;

AQUIFEX AEOLICUS; ARTICLE; CATALYST; CHEMICAL REACTION; CLUSTER ANALYSIS; CONTROLLED STUDY; DEUTERON NUCLEAR MAGNETIC RESONANCE; ELECTRON NUCLEAR DOUBLE RESONANCE; ELECTRON SPIN RESONANCE; ENZYME ACTIVE SITE; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; NONHUMAN; PH; PHOSPHORUS NUCLEAR MAGNETIC RESONANCE; POINT MUTATION; PRIORITY JOURNAL; WILD TYPE;

BINDING SITES; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; IRON; MUTANT PROTEINS; MUTATION; ORGANOPHOSPHORUS COMPOUNDS; OXIDOREDUCTASES; SPECTRUM ANALYSIS; SULFUR;

EID: 84862528394     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi3001215     Document Type: Article

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