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Tracking the route of molecular oxygen in O-2-tolerant membrane-bound [NiFe] hydrogenase
Zitatschlüssel ISI:000426671900013
Autor 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
Seiten E2229-E2237
Jahr 2018
ISSN 0027-8424
DOI 10.1073/pnas.1712267115
Adresse 2101 CONSTITUTION AVE NW, WASHINGTON, DC 20418 USA
Journal PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Jahrgang 115
Nummer 10
Monat MAR 6
Verlag NATL ACAD SCIENCES
Zusammenfassung [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.
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