Investigating the intermediates in the reaction of ribonucleoside triphosphate reductase from Lactobacillus leichmannii: An application of HF EPR-RFQ technology

Journal of Magnetic Resonance

Volumn 213, Issue 1, 2011, Pages 32-45

  Manzerova, Julia ^a   Krymov, Vladimir ^a   Gerfen, Gary J ^a  

^a ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

Author keywords

Active site; Adenosylcobalamin; Dipolar interaction; Electron paramagnetic resonance (EPR); Enzyme; Enzymology; Exchange interaction (J ex); Exchange coupled pair; High frequency (HF); Homolysis; Lactobacillus leichmannii; Rapid freeze quench (RFQ); Ribonucleoside triphosphate reductase (RTPR); Ribonucleotide reductase; Thiyl radical

Indexed keywords

ACTIVE SITE; ADENOSYLCOBALAMIN; DIPOLAR INTERACTION; ELECTRON PARAMAGNETIC RESONANCE (EPR); ENZYMOLOGY; EXCHANGE-COUPLED PAIR; HIGH FREQUENCY HF; HOMOLYSIS; LACTOBACILLUS LEICHMANNII; RAPID FREEZE-QUENCH (RFQ); RIBONUCLEOSIDES; RIBONUCLEOTIDE REDUCTASE; THIYL RADICALS;

ELECTRON RESONANCE; ELECTRON SPIN RESONANCE SPECTROSCOPY; ENZYMES; INNOVATION; PARAMAGNETIC MATERIALS; PARAMAGNETISM; REACTION INTERMEDIATES; SPECTROSCOPY;

PARAMAGNETIC RESONANCE;

CYANOCOBALAMIN; DYES, REAGENTS, INDICATORS, MARKERS AND BUFFERS; RIBONUCLEOSIDE TRIPHOSPHATE REDUCTASE; RIBONUCLEOSIDE-TRIPHOSPHATE REDUCTASE; RIBONUCLEOTIDE REDUCTASE;

ALGORITHM; ANAEROBIC GROWTH; ANISOTROPY; ARTICLE; BACTERIAL GENE; CHEMISTRY; ELECTROMAGNETIC FIELD; ELECTRON SPIN RESONANCE; ENZYME ACTIVE SITE; ENZYMOLOGY; FREEZING; GENETICS; INSTRUMENTATION; LACTOBACILLUS LEICHMANNII; METHODOLOGY; PLASMID; POWDER; TEMPERATURE;

ALGORITHMS; ANAEROBIOSIS; ANISOTROPY; CATALYTIC DOMAIN; ELECTROMAGNETIC FIELDS; ELECTRON SPIN RESONANCE SPECTROSCOPY; FREEZING; GENES, BACTERIAL; INDICATORS AND REAGENTS; LACTOBACILLUS LEICHMANNII; PLASMIDS; POWDERS; RIBONUCLEOTIDE REDUCTASES; TEMPERATURE; VITAMIN B 12;

LACTOBACILLUS LEICHMANNII; PROKARYOTA;

EID: 80055080499     PISSN: 10907807     EISSN: 10960856     Source Type: Journal    
DOI: 10.1016/j.jmr.2011.08.030     Document Type: Article

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