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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America. >Tracking the route of molecular oxygen in O-2-tolerant membrane-bound NiFe hydrogenase
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Tracking the route of molecular oxygen in O-2-tolerant membrane-bound NiFe hydrogenase

机译：Tracking the route of molecular oxygen in O-2-tolerant membrane-bound NiFe hydrogenase

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摘要

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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