pH rate profiles of FnY356-R2s (n = 2, 3, 4) in Escherichia coli ribonucleotide reductase: Evidence that Y356 is a redox-active amino acid along the radical propagation pathway

Journal of the American Chemical Society

Volumn 128, Issue 5, 2006, Pages 1562-1568

  Seyedsayamdost, Mohammad R ^a   Yee, Cyril S ^a   Reece, Steven Y ^a   Nocera, Daniel G ^a   Stubbe, JoAnne ^a  

^a MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CATALYSIS; ENZYMES; PH EFFECTS; REDOX REACTIONS; SUBSTRATES; SYNTHESIS (CHEMICAL);

FLUORINATED TYROSINE DERIVATIVES; RADICAL PROPAGATION PATHWAY; RADICAL PROPAGATION PROCESS; RIBONUCLEOTIDE REDUCTASE (RNR);

ESCHERICHIA COLI;

AMINO ACID; CYSTEINE; DEOXYRIBONUCLEOTIDE; NUCLEOTIDE DERIVATIVE; RADICAL; RIBONUCLEOTIDE REDUCTASE; TYROSINE DERIVATIVE;

AMINO ACID SUBSTITUTION; ARTICLE; ENZYME ANALYSIS; ENZYME MECHANISM; ENZYME SUBUNIT; ESCHERICHIA COLI; FLUORINATION; HYDROGEN BOND; MOLECULAR MODEL; NONHUMAN; OXIDATION REDUCTION POTENTIAL; OXIDATION REDUCTION REACTION; PH; TECHNOLOGY;

ESCHERICHIA COLI; HYDROGEN-ION CONCENTRATION; KINETICS; MODELS, MOLECULAR; OXIDATION-REDUCTION; RIBONUCLEOTIDE REDUCTASES; TYROSINE;

EID: 32244433011     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja055927j     Document Type: Article

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