Development of a cell-free system reveals an oxygen-labile step in the maturation of [NiFe]-hydrogenase 2 of Escherichia coli |
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Authors: | Basem Soboh |
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Affiliation: | Institute for Mikrobiologie, Martin-Luther University Halle-Wittenberg, 06120 Halle (Saale), Germany |
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Abstract: | By combining extracts from strains lacking genes encoding either the maturation enzymes or the large subunits of hydrogenases 1, 2 and 3 we could reconstitute in vitro under strictly anaerobic conditions 10-15% of the hydrogenase activity present in wild type Escherichia coli extracts. Purified, unprocessed Strep-tagged variants of the hydrogenase 2 large subunit, HybC, isolated from either a ΔhybD (encoding the hydrogenase 2-specific protease) mutant or a strain deficient in HypF could also be matured to active, processed enzyme using this system. These studies reveal that minimally one step early on the hydrogenase maturation pathway is oxygen-labile. |
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Keywords: | [NiFe]-hydrogenase In vitro processing Hydrogen oxidation Hyp maturation proteins |
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