Bioluminescence is produced from a trapped firefly luciferase conformation predicted by the domain alternation mechanism

Journal of the American Chemical Society

Volumn 133, Issue 29, 2011, Pages 11088-11091

  Branchini, Bruce R ^a   Rosenberg, Justin C ^a   Fontaine, Danielle M ^a   Southworth, Tara L ^a   Behney, Curran E ^a   Uzasci, Lerna ^a  

^a The Holleran Center for Community Action and Public Policy   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; ACYL-COA; ADENYLATE; C-DOMAIN; CYSTEINE RESIDUES; FIREFLY LUCIFERASE; HALF-REACTIONS; OXIDATIVE PROCESS; SYNTHETASES; THIOESTERS;

AMINO ACIDS; BIOLUMINESCENCE; CATALYSTS; CONFORMATIONS; CRYSTAL STRUCTURE; ENZYMES; ETHANE; PHOSPHORESCENCE;

PLANTS (BOTANY);

CHYMOTRYPSIN; CYSTEINE; ELASTASE; FIREFLY LUCIFERASE; LUCIFERIN; N ETHYLMALEIMIDE; THERMOLYSIN;

ADENYLATION; ARTICLE; BIOLUMINESCENCE; CONTROLLED STUDY; CROSS LINKING; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME MECHANISM; ENZYME METABOLISM; PROTEIN DEGRADATION;

AMINO ACID SEQUENCE; ANIMALS; FIREFLIES; FIREFLY LUCIFERIN; LUCIFERASES, FIREFLY; LUMINESCENCE; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY;

EID: 79960599223     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja2041496     Document Type: Article

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