Identification and Characterization of the "Super-Reduced" State of the H-Cluster in [FeFe] Hydrogenase: A New Building Block for the Catalytic Cycle?

Super‐reduced and super‐active: A new redox state in the active site of algal [FeFe] hydrogenases has been identified and characterized by EPR and FTIR spectroscopy. Electrochemical and in vitro essays show that this species is highly active in hydrogen production and suggest that it is a key interm...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	Angewandte Chemie International Edition 2012-11, Vol.51 (46), p.11458-11462
Hauptverfasser:	Adamska, Agnieszka, Silakov, Alexey, Lambertz, Camilla, Rüdiger, Olaf, Happe, Thomas, Reijerse, Edward, Lubitz, Wolfgang
Format:	Artikel
Sprache:	eng
Schlagworte:	biohydrogen Catalytic Domain Clostridium acetobutylicum - chemistry Clostridium acetobutylicum - enzymology Clostridium acetobutylicum - metabolism electron spin resonance Electron Spin Resonance Spectroscopy Enzyme Activation FTIR spectroscopy Hydrogen - metabolism hydrogenase Hydrogenase - chemistry Hydrogenase - metabolism Oxidation-Reduction protein film electrochemistry Spectroscopy, Fourier Transform Infrared
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Beschreibung
Zusammenfassung:	Super‐reduced and super‐active: A new redox state in the active site of algal [FeFe] hydrogenases has been identified and characterized by EPR and FTIR spectroscopy. Electrochemical and in vitro essays show that this species is highly active in hydrogen production and suggest that it is a key intermediate in the catalytic cycle of all [FeFe] hydrogenases.
ISSN:	1433-7851 1521-3773
DOI:	10.1002/anie.201204800