direkt zum Inhalt springen

direkt zum Hauptnavigationsmenü

Sie sind hier

TU Berlin

Page Content

Publications

Tracking the route of molecular oxygen in O-2-tolerant membrane-bound [NiFe] hydrogenase
Citation key ISI:000426671900013
Author Kalms, Jacqueline and Schmidt, Andrea and Frielingsdorf, Stefan and Utesch, Tillmann and Gotthard, Guillaume and von Stetten, David and van der Linden, Peter and Royant, Antoine and Mroginski, Maria Andrea and Carpentier, Philippe and Lenz, Oliver and Scheerer, Patrick
Pages E2229-E2237
Year 2018
ISSN 0027-8424
DOI 10.1073/pnas.1712267115
Address 2101 CONSTITUTION AVE NW, WASHINGTON, DC 20418 USA
Journal PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 115
Number 10
Month MAR 6
Publisher NATL ACAD SCIENCES
Abstract [NiFe] hydrogenases catalyze the reversible splitting of H-2 into protons and electrons at a deeply buried active site. The catalytic center can be accessed by gas molecules through a hydrophobic tunnel network. While most [NiFe] hydrogenases are inactivated by O-2, a small subgroup, including the membrane-bound [NiFe] hydrogenase (MBH) of Ralstonia eutropha, is able to overcome aerobic inactivation by catalytic reduction of O-2 to water. This O2 tolerance relies on a special [4Fe3S] cluster that is capable of releasing two electrons upon O-2 attack. Here, the O2 accessibility of the MBH gas tunnel network has been probed experimentally using a ``soak-and-freeze'' derivatization method, accompanied by protein X-ray crystallography and computational studies. This combined approach revealed several sites of O-2 molecules within a hydrophobic tunnel network leading, via two tunnel entrances, to the catalytic center of MBH. The corresponding site occupancies were related to the O-2 concentrations used for MBH crystal derivatization. The examination of the O-2-derivatized data furthermore uncovered two unexpected structural alterations at the [4Fe3S] cluster, which might be related to the O-2 tolerance of the enzyme.
Bibtex Type of Publication Article
Download Bibtex entry

Zusatzinformationen / Extras

Quick Access:

Schnellnavigation zur Seite über Nummerneingabe

Auxiliary Functions

This site uses Matomo for anonymized webanalysis. Visit Data Privacy for more information and opt-out options.