Preserved catalytic activity in an engineered ribonucleotide reductase R2 protein with a nonphysiological radical transfer pathway: The importance of hydrogen bond connections between the participating residues

Journal of Biological Chemistry

Volumn 273, Issue 33, 1998, Pages 21003-21008

  Ekberg, Monica ^a   Pötsch, Stephan ^a   Sandin, Elin ^a   Thunnissen, Marjolein ^a   Nordlund, Pär ^a   Sahlin, Margareta ^a   Sjöberg, Britt Marie ^a  

^a STOCKHOLM UNIVERSITY   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

RIBONUCLEOTIDE REDUCTASE;

ARTICLE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME CONFORMATION; ENZYME SPECIFICITY; ESCHERICHIA COLI; HYDROGEN BOND; NONHUMAN; PHYLOGENY; PRIORITY JOURNAL; PROTON TRANSPORT; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION;

AMINO ACID SUBSTITUTION; ASPARAGINE; ASPARTIC ACID; CATALYSIS; ESCHERICHIA COLI; FREE RADICALS; GLUTAMIC ACID; HYDROGEN BONDING; IRON; PROTEIN BINDING; PROTEIN ENGINEERING; RIBONUCLEOTIDE REDUCTASES; TYROSINE;

EID: 0032516890     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.273.33.21003     Document Type: Article

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