Mutation of the conserved Cys165 outside of the CuA domain destabilizes nitrous oxide reductase but maintains its catalytic activity Evidence for disulfide bridges and a putative protein disulfide isomerase gene

European Journal of Biochemistry

Volumn 237, Issue 2, 1996, Pages 447-453

  Dreusch, Andreas ^a   Riester, Joachim ^b   Kroneck, Peter M H ^b   Zumft, Walter G ^a  

^a UNIVERSITY OF KARLSRUHE   (Germany)

^b UNIVERSITY OF KONSTANZ   (Germany)

Author keywords

Copper protein; Disulfide bond; Nitrous oxide reductase; Protein disulfide isomerase; Site directed mutagenesis

Indexed keywords

NITROUS OXIDE REDUCTASE;

AMINO ACID SEQUENCE; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME STABILITY; GENETIC ANALYSIS; NONHUMAN; OPEN READING FRAME; POINT MUTATION; PRIORITY JOURNAL; PSEUDOMONAS STUTZERI;

AMINO ACID SEQUENCE; BASE SEQUENCE; CATALYSIS; CONSERVED SEQUENCE; CYSTEINE; DISULFIDES; DNA PRIMERS; DNA, BACTERIAL; ENZYME STABILITY; GENES, BACTERIAL; ISOMERASES; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; MUTAGENESIS, SITE-DIRECTED; OPEN READING FRAMES; OXIDOREDUCTASES; POINT MUTATION; PROTEIN DISULFIDE-ISOMERASE; PSEUDOMONAS; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 0029978149     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.0447k.x     Document Type: Article

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