An engineered two-iron superoxide reductase lacking the [Fe(SCys)4] site retains its catalytic properties in vitro and in vivo

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

Volumn 100, Issue 7, 2003, Pages 3802-3807

  Emerson, Joseph P ^a   Cabelli, Diane E ^b   Kurtz Jr , Donald M ^a  

^a UNIVERSITY OF GEORGIA   (United States)

^b BROOKHAVEN NATIONAL LABORATORY   (United States)

Author keywords

1Fe SOR; 2Fe SOR; Oxidative stress; Pulse radiolysis

Indexed keywords

BACTERIAL ENZYME; CYSTEINE; IRON; LIGAND; SERINE; SUPEROXIDE REDUCTASE; UNCLASSIFIED DRUG; IRON SULFUR PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; OXIDOREDUCTASE; RECOMBINANT PROTEIN;

AEROBIC METABOLISM; AMINO ACID SUBSTITUTION; ANAEROBIC BACTERIUM; ARCHAEBACTERIUM; ARTICLE; BACTERIAL GROWTH; CATALYSIS; DESULFOVIBRIO VULGARIS; ELECTRON TRANSPORT; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ESCHERICHIA COLI; IN VITRO STUDY; IN VIVO STUDY; OXIDATION REDUCTION REACTION; OXIDATIVE STRESS; PRIORITY JOURNAL; PROTEIN FUNCTION; PULSE RADIOLYSIS; SPECTROSCOPY; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYMOLOGY; GROWTH, DEVELOPMENT AND AGING; KINETICS; METABOLISM; PROTEIN ENGINEERING; PROTEIN SECONDARY STRUCTURE; SITE DIRECTED MUTAGENESIS;

ARCHAEA; BACTERIA (MICROORGANISMS); DESULFOVIBRIO; DESULFOVIBRIO VULGARIS; ESCHERICHIA COLI; NEGIBACTERIA;

AEROBIOSIS; AMINO ACID SUBSTITUTION; ARCHAEA; BACTERIA, ANAEROBIC; BINDING SITES; CATALYSIS; ESCHERICHIA COLI; IRON-SULFUR PROTEINS; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; NADP; OXIDOREDUCTASES; PROTEIN ENGINEERING; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS;

EID: 0037389525     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0537177100     Document Type: Article

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