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

Morra, Simone; Arizzi, Mariaconcetta; Valetti, Francesca; Gilardi, Gianfranco

Abstract

© 2016 American Chemical Society. The newly isolated Clostridium beijerinckii [FeFe]-hydrogenase CbA5H was characterized by Fourier transform infrared spectroscopy coupled to enzymatic 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 challenging perspectives on the oxygen sensitivity mechanism as well as new possibilities for exploitation in industrial applications.

Citation

Morra, S., Arizzi, M., Valetti, F., & Gilardi, G. (2016). Oxygen Stability in the New [FeFe]-Hydrogenase from Clostridium beijerinckii SM10 (CbA5H). Biochemistry, 55(42), 5897-5900. https://doi.org/10.1021/acs.biochem.6b00780

• Journal Article Type: Article
• Acceptance Date: Oct 13, 2016
• Online Publication Date: Oct 17, 2016
• Publication Date: Oct 25, 2016
• Deposit Date: Jan 31, 2020
• Publicly Available Date: Feb 11, 2020
• Journal: Biochemistry
• Electronic ISSN: 1520-4995
• Publisher: American Chemical Society
• Peer Reviewed: Peer Reviewed
• Volume: 55
• Issue: 42
• Pages: 5897-5900
• DOI: https://doi.org/10.1021/acs.biochem.6b00780
• Public URL: https://nottingham-repository.worktribe.com/output/3841157
• Publisher URL: https://pubs.acs.org/doi/10.1021/acs.biochem.6b00780
• Additional Information: This document is the Accepted Manuscript version of a Published Work that appeared in final form in Biochemistry ,copyright©American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see https://pubs.acs.org/doi/10.1021/acs.biochem.6b00780