The newly isolated [FeFe]-hydrogenase CbA5H was characterized by FTIR spectroscopy coupled to enzy-matic activity assays. This showed for the first time that in this enzyme the oxygen-sensitive active state Hox can be simply and reversibly converted to the oxygen-stable inactive Hinact state. This suggests that oxygen sensitivity is not an intrinsic feature of the catalytic center of [FeFe]-hydrogenases (H-cluster), opening new challeng-ing perspectives on the oxygen sensitivity mechanism as well as new possibilities for the exploitation in industri-al applications.

Oxygen Stability in the New [FeFe]-Hydrogenase from Clostridium beijerinckii SM10 (CbA5H)

MORRA, SIMONE;ARIZZI, MARIACONCETTA;VALETTI, Francesca;GILARDI, Gianfranco
2016

Abstract

The newly isolated [FeFe]-hydrogenase CbA5H was characterized by FTIR spectroscopy coupled to enzy-matic activity assays. This showed for the first time that in this enzyme the oxygen-sensitive active state Hox can be simply and reversibly converted to the oxygen-stable inactive Hinact state. This suggests that oxygen sensitivity is not an intrinsic feature of the catalytic center of [FeFe]-hydrogenases (H-cluster), opening new challeng-ing perspectives on the oxygen sensitivity mechanism as well as new possibilities for the exploitation in industri-al applications.
BIOCHEMISTRY
55
42
5897
5900
http://pubs.acs.org/journal/bichaw
Biochemistry
Morra, Simone; Arizzi, Mariaconcetta; Valetti, Francesca; Gilardi, Gianfranco
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/2318/1612875
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