Authors
Giorgio Caserta, Sven Hartmann, Casey Van Stappen, Chara Karafoulidi-Retsou, Christian Lorent, Stefan Yelin, Matthias Keck, Janna Schoknecht, Ilya Sergueev, Yoshitaka Yoda, Peter Hildebrandt, Christian Limberg, Serena DeBeer, Ingo Zebger, Stefan Frielingsdorf, Oliver Lenz
Publication date
2023/4
Journal
Nature chemical biology
Volume
19
Issue
4
Pages
498-506
Publisher
Nature Publishing Group US
Description
[NiFe]-hydrogenases are biotechnologically relevant enzymes catalyzing the reversible splitting of H2 into 2e− and 2H+ under ambient conditions. Catalysis takes place at the heterobimetallic NiFe(CN)2(CO) center, whose multistep biosynthesis involves careful handling of two transition metals as well as potentially harmful CO and CN− molecules. Here, we investigated the sequential assembly of the [NiFe] cofactor, previously based on primarily indirect evidence, using four different purified maturation intermediates of the catalytic subunit, HoxG, of the O2-tolerant membrane-bound hydrogenase from Cupriavidus necator. These included the cofactor-free apo-HoxG, a nickel-free version carrying only the Fe(CN)2(CO) fragment, a precursor that contained all cofactor components but remained redox inactive and the fully mature HoxG. Through biochemical analyses combined with comprehensive spectroscopic …
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Scholar articles
G Caserta, S Hartmann, C Van Stappen… - Nature chemical biology, 2023