O 2 reactions at the six-iron active site (H-cluster) in [FeFe]-hydrogenase

Journal of Biological Chemistry

Volumn 286, Issue 47, 2011, Pages 40614-40623

  Lambertz, Camilla ^a   Leidel, Nils ^b   Havelius, Kajsa G V ^b   Noth, Jens ^a   Chernev, Petko ^b   Winkler, Martin ^a   Happe, Thomas ^a   Haumann, Michael ^b  

^a RUHR UNIVERSITY BOCHUM   (Germany)

^b FREIE UNIVERSITÄT BERLIN   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

[FEFE]HYDROGENASES; ACTIVE SITE; CHLAMYDOMONAS REINHARDTII; DIFFUSION PATHS; EXPOSURE PERIOD; EXTENDED X-RAY ABSORPTION FINE STRUCTURE SPECTRUM; GREEN ALGA; H-CLUSTER; HYDROGENASES; INDUCED DEGRADATION; IRON IONS; IRON OXIDATION; IRREVERSIBLE INHIBITIONS; KINETIC ANALYSIS; PROTEIN SAMPLES; REACTION SEQUENCES; REACTIVE OXYGEN; REDOX POTENTIALS; SECOND PHASE; SUPEROXIDES; THREE PHASIS; TIME-RESOLVED; X-RAY ABSORPTION NEAR-EDGE STRUCTURE;

ABSORPTION SPECTRA; EXTENDED X RAY ABSORPTION FINE STRUCTURE SPECTROSCOPY; GALLIUM ALLOYS; GENETIC ENGINEERING; HYDROGEN; IRON; IRON COMPOUNDS; METAL IONS; MOLECULAR OXYGEN; OXIDATION; OXYGENATION; REDOX REACTIONS; X RAY ABSORPTION NEAR EDGE STRUCTURE SPECTROSCOPY; X RAY ABSORPTION SPECTROSCOPY;

IRON ALLOYS;

IRON HYDROGENASE; OXYGEN; REACTIVE OXYGEN METABOLITE; SUPEROXIDE; HYDROGENASE; IRON; IRON SULFUR PROTEIN;

ARTICLE; CHEMICAL MODIFICATION; CHEMICAL REACTION; CHLAMYDOMONAS REINHARDTII; CONTROLLED STUDY; DIFFUSION; ENZYME ACTIVE SITE; ENZYME DEGRADATION; ENZYME KINETICS; ENZYME METABOLISM; ENZYME STRUCTURE; EXPOSURE; NONHUMAN; OXIDATION REDUCTION POTENTIAL; PRIORITY JOURNAL; X RAY ABSORPTION SPECTROSCOPY; CHEMISTRY; DRUG EFFECT; ENZYME ACTIVATION; ENZYMOLOGY; KINETICS; METABOLISM; PROTEIN BINDING;

CHLAMYDOMONAS REINHARDTII; CHLOROPHYTA;

CATALYTIC DOMAIN; CHLAMYDOMONAS REINHARDTII; ENZYME ACTIVATION; HYDROGENASE; IRON; IRON-SULFUR PROTEINS; KINETICS; OXYGEN; PROTEIN BINDING; REACTIVE OXYGEN SPECIES; X-RAY ABSORPTION SPECTROSCOPY;

EID: 81755171433     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.283648     Document Type: Article

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