Please use this identifier to cite or link to this item: http://dx.doi.org/10.14279/depositonce-6248
Main Title: Reactivation from the Ni-B state in [NiFe] hydrogenase of Ralstonia eutropha is controlled by reduction of the superoxidised proximal cluster
Author(s): Radu, Valentin
Frielingsdorf, Stefan
Lenz, Oliver
Jeuken, Lars J. C.
Type: Article
Language Code: en
Abstract: The tolerance towards oxic conditions of O-2-tolerant [NiFe] hydrogenases has been attributed to an unusual [4Fe-3S] cluster that lies proximal to the [NiFe] active site. Upon exposure to oxygen, this cluster converts to a superoxidised (5+) state, which is believed to secure the formation of the so-called Ni-B state that is rapidly reactivated under reducing conditions. Here, the reductive reactivation of the membrane-bound [NiFe]-hydrogenase (MBH) from Ralstonia eutropha in a native-like lipid membrane was characterised and compared to a variant that instead carries a typical [4Fe-4S] proximal cluster. Reactivation from the Ni-B state was faster in the [4Fe-4S] variant, suggesting that the reactivation rate in MBH is limited by the reduction of the superoxidised [4Fe-3S] cluster. We propose that the [4Fe-3S] cluster plays a major role in protecting MBH by blocking the reversal of electron transfer to the [NiFe] active site, which would produce damaging radical oxygen species.
URI: https://depositonce.tu-berlin.de//handle/11303/6909
http://dx.doi.org/10.14279/depositonce-6248
Issue Date: 2016
Date Available: 24-Oct-2017
DDC Class: 540 Chemie und zugeordnete Wissenschaften
Sponsor/Funder: EC/FP7/280518/EU/Membrane-modified Electrodes to study Membrane Enzymes
DFG, EXC 314, Unifying Concepts in Catalysis
Creative Commons License: https://creativecommons.org/licenses/by/3.0/
Journal Title: Chemical communications
Publisher: Royal Society of Chemistry
Publisher Place: Cambridge
Volume: 52
Issue: 12
Publisher DOI: 10.1039/c5cc10382g
Page Start: 2632
Page End: 2635
EISSN: 1364-548X
ISSN: 1359-7345
Appears in Collections:Fachgebiet Physikalische Chemie / Biophysikalische Chemie » Publications

Files in This Item:
File SizeFormat 
c5cc10382g.pdf1.73 MBAdobe PDFView/Open


This item is licensed under a Creative Commons License Creative Commons