Identification and characterization of the "super-reduced" state of the H-cluster in [FeFe] hydrogenase: A new building block for the catalytic cycle?

Angewandte Chemie - International Edition

Volumn 51, Issue 46, 2012, Pages 11458-11462

  Adamska, Agnieszka ^a   Silakov, Alexey ^a   Lambertz, Camilla ^b   Rüdiger, Olaf ^a   Happe, Thomas ^b   Reijerse, Edward ^a   Lubitz, Wolfgang ^a  

^a MAX PLANCK INSTITUTE FOR CHEMICAL ENERGY CONVERSION   (Germany)

^b RUHR UNIVERSITY BOCHUM   (Germany)

Author keywords

biohydrogen; electron spin resonance; FTIR spectroscopy; hydrogenase; protein film electrochemistry

Indexed keywords

[FEFE]HYDROGENASES; ACTIVE SITE; BIO-HYDROGEN; BUILDING BLOCKES; CATALYTIC CYCLES; FTIR SPECTROSCOPY; H-CLUSTER; HYDROGENASES; IN-VITRO; PROTEIN FILMS; REDOX STATE;

FOURIER TRANSFORM INFRARED SPECTROSCOPY; HYDROGEN PRODUCTION; PARAMAGNETIC RESONANCE;

ELECTROCHEMISTRY;

HYDROGEN; HYDROGENASE;

ARTICLE; CHEMISTRY; CLOSTRIDIUM ACETOBUTYLICUM; ELECTRON SPIN RESONANCE; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYMOLOGY; INFRARED SPECTROSCOPY; METABOLISM; OXIDATION REDUCTION REACTION;

CATALYTIC DOMAIN; CLOSTRIDIUM ACETOBUTYLICUM; ELECTRON SPIN RESONANCE SPECTROSCOPY; ENZYME ACTIVATION; HYDROGEN; HYDROGENASE; OXIDATION-REDUCTION; SPECTROSCOPY, FOURIER TRANSFORM INFRARED;

EID: 84868533696     PISSN: 14337851     EISSN: 15213773     Source Type: Journal    
DOI: 10.1002/anie.201204800     Document Type: Article

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