ArticleNature chemical biology2016
Mechanism of hydrogen activation by [NiFe] hydrogenases.
Article in Nature chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed, 126 citations in OpenAlex.
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- Synthesis, Properties, and Electrochemical Proton Reduction of a Homoleptic Tetrathiolato Ni-Site Model of [NiFe]-Hydrogenase.Inorganic chemistry · 2025Article
- Fully Oxidized State of the Oxygen-Tolerant [NiFe] Hydrogenase fromInorganic chemistry · 2025Article
- Understanding the role of negative charge in the scaffold of an artificial enzyme for COJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024Article
- Replacing a Cysteine Ligand by Selenocysteine in a [NiFe]-Hydrogenase Unlocks Hydrogen Production Activity and Addresses the Role of Concerted Proton-Coupled Electron Transfer in Electrocatalytic Reversibility.Journal of the American Chemical Society · 2024Article
- DONSON facilitates Cdc45 and GINS chromatin association and is essential for DNA replication initiation.Nucleic acids research · 2023Article
- Comprehensive structural, infrared spectroscopic and kinetic investigations of the roles of the active-site arginine in bidirectional hydrogen activation by the [NiFe]-hydrogenase 'Hyd-2' fromChemical science · 2023Article
- Enzymatic and Bioinspired Systems for Hydrogen Production.International journal of molecular sciences · 2023Review
- Synthetic engineering of a new biocatalyst encapsulating [NiFe]-hydrogenases for enhanced hydrogen production.Journal of materials chemistry. B · 2023Article
- Non-Covalent Integration of a [FeFe]-Hydrogenase Mimic to Multiwalled Carbon Nanotubes for Electrocatalytic Hydrogen Evolution.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
- Structure of the membrane-bound formate hydrogenlyase complex from Escherichia coli.Nature communications · 2022Article
- Second and Outer Coordination Sphere Effects in Nitrogenase, Hydrogenase, Formate Dehydrogenase, and CO Dehydrogenase.Chemical reviews · 2022Review
- Conformational and mechanical stability of the isolated large subunit of membrane-bound [NiFe]-hydrogenase fromFrontiers in microbiology · 2022Article
- Harnessing selenocysteine to enhance microbial cell factories for hydrogen production.Frontiers in catalysis · 2022Article
- The crystalline state as a dynamic system: IR microspectroscopy under electrochemical control for a [NiFe] hydrogenase.Chemical science · 2021Article
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
The active site of [NiFe] hydrogenases contains a strictly conserved arginine that suspends a guanidine nitrogen atom <4.5 Å above the nickel and iron atoms. The guanidine headgroup interacts with the side chains of two conserved aspartic acid residues to complete an outer-shell canopy that has thus far proved intractable to investigation by site-directed mutagenesis. Using hydrogenase-1 from Escherichia coli, the strictly conserved residues R509 and D574 have been replaced by lysine (R509K) and asparagine (D574N) and the highly conserved D118 has been replaced by alanine (D118A) or asparagine (D118N/D574N). Each enzyme variant is stable, and their [(RS)2Niμ(SR)2Fe(CO)(CN)2] inner coordination shells are virtually unchanged. The R509K variant had >100-fold lower activity than native enzyme. Conversely, the variants D574N, D118A and D118N/D574N, in which the position of the guanidine headgroup is retained, showed 83%, 26% and 20% activity, respectively. The special kinetic requirement for R509 implicates the suspended guanidine group as the general base in H2 activation by [NiFe] hydrogenases.
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