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O-2-Tolerant H-2 Activation by an Isolated Large Subunit of a [NiFe] Hydrogenase
Zitatschlüssel ISI:000444792900007
Autor Hartmann, Sven and Frielingsdorf, Stefan and Ciaccafava, Alexandre and Lorent, Christian and Fritsch, Johannes and Siebert, Elisabeth and Priebe, Jacqueline and Haumann, Michael and Zebger, Ingo and Lenz, Oliver
Seiten 5339-5349
Jahr 2018
ISSN 0006-2960
DOI 10.1021/acs.biochem.8b00760
Jahrgang 57
Nummer 36
Monat SEP 11
Zusammenfassung The catalytic properties of hydrogenases are nature's answer to the seemingly simple reaction H-2 reversible arrow 2H(+) + 2e(-). Members of the phylogenetically diverse subgroup of [NiFe] hydrogenases generally consist of at least two subunits, where the large subunit harbors the H-2-activating [NiFe] site and the small subunit contains iron-sulfur clusters mediating e(-) transfer. Typically, [NiFe] hydrogenases are susceptible to inhibition by O-2. Here, we conducted system minimization by isolating and analyzing the large subunit of one of the rare members of the group of O-2-tolerant [NiFe] hydrogenases, namely the preHoxG protein of the membrane-bound hydrogenase from Ralstonia eutropha. Unlike previous assumptions, preHoxG was able to activate H-2 as it clearly performed catalytic hydrogen/deuterium exchange. However, it did not execute the entire catalytic cycle described for [NiFe] hydrogenases. Remarkably, H-2 activation was performed by preHoxG even in the presence of O-2, although the unique [4Fe-3S] cluster located in the small subunit and described to be crucial for tolerance toward O-2 was absent. These findings challenge the current understanding of O-2 tolerance of [NiFe] hydrogenases. The applicability of this minimal hydrogenase in basic and applied research is discussed.
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