Oxygen tolerance of the H2-sensing [NiFe] hydrogenase from Ralstonia eutropha H16 is based on limited access of oxygen to the active site

Journal of Biological Chemistry

Volumn 280, Issue 25, 2005, Pages 23791-23796

  Buhrke, Thorsten ^a   Lenz, Oliver ^a   Krauss, Norbert ^b   Friedrich, Bärbel ^a  

^a HUMBOLDT UNIVERSITY   (Germany)

^b CHARITÉ UNIVERSITÄTSMEDIZIN BERLIN   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; DERIVATIVES; ENZYME INHIBITION; HYDROPHOBICITY; METABOLISM; MICROORGANISMS; MUTAGENESIS; OXYGEN;

HYDROGEN METABOLISM; INTRAMOLECULAR HYDROPHOBIC CAVITIES; MUTANT PROTEINS; PROTON REDUCTION;

ENZYMES;

HYDROGENASE; OXYGEN; PROTEIN NICKEL IRON HYDROGENASE; UNCLASSIFIED DRUG; NICKEL IRON HYDROGENASE; NICKEL-IRON HYDROGENASE; PRIMER DNA;

ARTICLE; BACTERIAL METABOLISM; CONTROLLED STUDY; ENZYME ACTIVE SITE; NONHUMAN; OXYGEN SENSING; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FUNCTION; SITE DIRECTED MUTAGENESIS; WAUTERSIA EUTROPHA; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYMOLOGY; METABOLISM; NUCLEOTIDE SEQUENCE; PROTEIN CONFORMATION;

ALLOCHROMATIUM VINOSUM; DESULFOVIBRIO GIGAS; WAUTERSIA EUTROPHA;

BASE SEQUENCE; BINDING SITES; CUPRIAVIDUS NECATOR; DNA PRIMERS; HYDROGENASE; MODELS, MOLECULAR; OXYGEN; PROTEIN CONFORMATION;

EID: 21244441201     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M503260200     Document Type: Article

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