Journal
ACS CATALYSIS
Volume 10, Issue 23, Pages 13890-13894Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acscatal.0c04079
Keywords
metalloenzyme; hydrogenase; hydrogen; nickel; iron; catalytic cycle; spectroscopy
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Funding
- Einstein Foundation Berlin [EVF-2016-277]
- Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) under Germany's Excellence Strategy [EXC2008-390540038]
- Einstein Center of Catalysis (EC2)/BIG-NSE
- EU [810856]
- NIH [GM-65440]
- SPring-8 proposal [2017B1321, 2019A1201]
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[NiFe]-hydrogenases catalyze the reversible reac- tion H-2 reversible arrow 2Fr + 2e(.)(-) Their basic module consists of a large subunit, coordinating the NiFe(CO)(CN)(2) center, and a small subunit that carries electron-transferring iron-sulfur clusters. Here, we report the in vitro assembly of fully functional [NiFe]-hydrogenase starting from the isolated large and small subunits. Activity assays complemented by spectroscopic measurements revealed a native-like hydrogenase. This approach was used to label exclusively the NiFe(CO)(CN)(2) center with Fe-57, enabling a clear view of the catalytic site by means of nuclear resonance vibrational spectroscopy. This strategy paves the way for in-depth studies of [NiFe]-hydrogenase catalytic intermediates.
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