EPR and FTIR analysis of the mechanism of H2 activation by [FeFe]-hydrogenase hyda1 from chlamydomonas reinhardtii

Journal of the American Chemical Society

Volumn 135, Issue 18, 2013, Pages 6921-6929

  Mulder, David W ^a   Ratzloff, Michael W ^a   Shepard, Eric M ^b   Byer, Amanda S ^b   Noone, Seth M ^a   Peters, John W ^b   Broderick, Joan B ^b   King, Paul W ^a  

^a NATIONAL RENEWABLE ENERGY LABORATORY   (United States)

^b MONTANA STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

[FEFE]HYDROGENASES; BIOPHYSICAL PROPERTIES; CHLAMYDOMONAS REINHARDTII; ELECTRON PARAMAGNETIC RESONANCE SPECTROSCOPY; ELECTRON TRANSFER; RELAXATION PROPERTY; SODIUM DITHIONITE; STRUCTURAL REARRANGEMENT;

AMINO ACIDS; ELECTRON SPIN RESONANCE SPECTROSCOPY; FOURIER TRANSFORM INFRARED SPECTROSCOPY; LIGANDS; MAGNETIC RESONANCE; ORGANOMETALLICS; OXIDATION; PARAMAGNETISM;

REDUCTION;

ALGAL PROTEIN; CYSTEINE; HYDROGEN; IRON HYDROGENASE; IRON HYDROGENASE A1; PROTON; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; CHLAMYDOMONAS REINHARDTII; CONTROLLED STUDY; ELECTRON SPIN RESONANCE; ELECTRON TRANSPORT; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME MECHANISM; ENZYME METABOLISM; ENZYME STRUCTURE; INFRARED SPECTROSCOPY; NONHUMAN; REACTION ANALYSIS;

CHLAMYDOMONAS REINHARDTII; ELECTRON SPIN RESONANCE SPECTROSCOPY; ENZYME ACTIVATION; HYDROGEN; HYDROGENASE; IRON-SULFUR PROTEINS; MODELS, MOLECULAR; MOLECULAR CONFORMATION; SPECTROSCOPY, FOURIER TRANSFORM INFRARED;

EID: 84877255197     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja4000257     Document Type: Article

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