Modular behavior of tauD provides insight into the origin of specificity in α-ketoglutarate-dependent nonheme iron oxygenases

Proceedings of the National Academy of Sciences of the United States of America

Volumn 106, Issue 47, 2009, Pages 19791-19795

  McCusker, Kevin P ^a   Klinman, Judith P ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Enzyme modularity; Hydrogen transfer; Oxygen activation

Indexed keywords

2 OXOGLUTARIC ACID; CARBON; HYDROGEN; IRON; OXYGEN; OXYGENASE; TAURINE ALPHA KETOGLUTARATE DIOXYGENASE; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; DECARBOXYLATION; ELECTRON; ENZYME STRUCTURE; OXIDATION; OXYGEN AFFINITY; OXYGEN CONSUMPTION; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS; STOICHIOMETRY;

CATALYTIC DOMAIN; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; IRON; KETOGLUTARIC ACIDS; MIXED FUNCTION OXYGENASES; MUTAGENESIS, SITE-DIRECTED; OXIDATION-REDUCTION; OXYGEN; OXYGENASES; PROTEIN CONFORMATION; SUBSTRATE SPECIFICITY; SUCCINIC ACID; SULFITES; UNCOUPLING AGENTS;

EID: 73949125232     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0910660106     Document Type: Article

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