Characterization of a putative sensory [FeFe]-hydrogenase provides new insight into the role of the active site architecture

2020/01/01 by Henrik Land, Alina Sekretareva, Ping Huang +7 · 1 voice · 3 citations
Energy · Engineering · #Advanced battery technologies research #Electrocatalysts for Energy Conversion #Metalloenzymes and iron-sulfur proteins

paper · pdf · doi:10.1039/d0sc03319g

openalex publication_date 2020/01/01 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/01

Abstract

interconversion, and unusual reactivity towards known hydrogenase inhibitors. These properties are related to differences in active site architecture between the M2e [FeFe]-hydrogenase and "prototypical" [FeFe]-hydrogenases. Thus, this study provides new insight into the role of this subclass in hydrogen metabolism and the influence of the active site pocket on the chemistry of the H-cluster.

Cited by

• Insights into the Molecular Mechanism of Formaldehyde Inhibition of [FeFe]-Hydrogenases
• Oxygen sensitivity of [FeFe]-hydrogenase: a comparative study of active site mimics inside vs. outside the enzyme
• Probing the Influence of the Protein Scaffold on H-Cluster Reactivity via Gain-of-Function Studies─Improved H2 Evolution and O2 Tolerance through Rational Design of [FeFe] Hydrogenase

Discussions

• Damn, time really does fly! I remember publishing in the ten-years-edition... doi.org/10.1039/D0SC... [bsky, 3 points, 0 comments]

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