ArticleAnalytical chemistry2025
Reconsidering the Enzyme Kinetics of [FeFe]-Hydrogenases: Improved Turnover Rates and New Insights into pH and Potential Dependence with Eu(II)-Based Solution Assays.
Article in Analytical chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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2 citing papers in PubMed.
- Beyond Canonical CO Oxidation: Structural and Evolutionary Insights Into a Non-Canonical Carbon Monoxide Dehydrogenase.Angewandte Chemie (International ed. in English) · 2026Article
- Probing the Role of Accessory FeS Clusters in Putative Sensory Group D [FeFe] Hydrogenase: Influence of the C-Terminal [4Fe-4S] Cluster on the Reactivity ofBiochemistry · 2026Article
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13 authors.
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Abstract
Metal-dependent redox enzymes are central for microbial processing of gases, as exemplified by hydrogenase, nitrogenase, and carbon monoxide dehydrogenase. Due to their remarkable efficiencies and high biotechnological relevance, such gas-processing enzymes are intensively studied. Nevertheless, many of their mechanistic details remain opaque. We herein report a new method for solution assays under reducing conditions based on europium(II) as a terminal reductant and show how it can be employed to gain new insight into hydrogenase kinetics. Compared with the commonly used reductant sodium dithionite, this work shows that Eu(II) can serve as a robust and relatively easy-to-handle alternative electron donor, also providing a larger potential window for catalytic studies. Further, this work clarifies previous discrepancies in the literature regarding the influence of pH on hydrogenase kinetics in these assays. Our study shows that sodium dithionite, most likely due to its decomposition into SO
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