Module fusion in an A-type flavoprotein from the cyanobacterium Synechocystis condenses a multiple-component pathway in a single polypeptide chain

Biochemical and Biophysical Research Communications

Volumn 294, Issue 1, 2002, Pages 82-87

  Vicente, João B ^a   Gomes, Cláudio M ^a,b   Wasserfallen, Alain ^c   Teixeira, Miguel ^a  

^a INSTITUTO DE TECNOLOGIA QUÍMICA E BIOLÓGICA   (Portugal)

^b UNIVERSIDADE NOVA DE LISBOA   (Portugal)

^c ETH ZURICH   (Switzerland)

Author keywords

A type flavoproteins; Diiron; Oxygen reductase

Indexed keywords

FLAVOPROTEIN; FLAVOPROTEIN TYPE A; OXYGEN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE; UNCLASSIFIED DRUG; WATER;

AMINO ACID SEQUENCE; ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; CYANOBACTERIUM; ELECTRON TRANSPORT; ENZYME ACTIVITY; KINETICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN PURIFICATION; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS;

AMINO ACID SEQUENCE; CYANOBACTERIA; ELECTRON TRANSPORT; FLAVIN MONONUCLEOTIDE; FLAVIN-ADENINE DINUCLEOTIDE; FLAVOPROTEINS; KINETICS; MODELS, CHEMICAL; MOLECULAR SEQUENCE DATA; SEQUENCE ALIGNMENT;

SYNECHOCYSTIS; SYNECHOCYSTIS SP.;

EID: 0036297346     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-291X(02)00434-5     Document Type: Article

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