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A unique iron-sulfur cluster is crucial for oxygen tolerance of a [NiFe]-hydrogenase.
Zitatschlüssel Goris2011
Autor Tobias Goris and Annemarie F Wait and Miguel Saggu and Johannes Fritsch and Nina Heidary and Matthias Stein and Ingo Zebger and Friedhelm Lendzian and Fraser A Armstrong and Bärbel Friedrich and Oliver Lenz
Seiten 310–318
Jahr 2011
DOI 10.1038/nchembio.555
Journal Nat Chem Biol
Jahrgang 7
Nummer 5
Monat May
Zusammenfassung Hydrogenases are essential for H(2) cycling in microbial metabolism and serve as valuable blueprints for H(2)-based biotechnological applications. However, most hydrogenases are extremely oxygen sensitive and prone to inactivation by even traces of O(2). The O(2)-tolerant membrane-bound [NiFe]-hydrogenase of Ralstonia eutropha H16 is one of the few examples that can perform H(2) uptake in the presence of ambient O(2). Here we show that O(2) tolerance is crucially related to a modification of the internal electron-transfer chain. The iron-sulfur cluster proximal to the active site is surrounded by six instead of four conserved coordinating cysteines. Removal of the two additional cysteines alters the electronic structure of the proximal iron-sulfur cluster and renders the catalytic activity sensitive to O(2) as shown by physiological, biochemical, spectroscopic and electrochemical studies. The data indicate that the mechanism of O(2) tolerance relies on the reductive removal of oxygenic species guided by the unique architecture of the electron relay rather than a restricted access of O(2) to the active site.
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