ArticleNature chemical biology2011
A unique iron-sulfur cluster is crucial for oxygen tolerance of a [NiFe]-hydrogenase.
Article in Nature chemical biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 73 papers.
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Who cites it
73 citing papers in PubMed, 255 citations in OpenAlex.
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- Glycerol-supplemented medium promotes transition of Cupriavidus necator from heterotrophic to lithoautotrophic growth.Biotechnology letters · 2025Article
- Red seaweed supplementation suppresses methanogenesis in the rumen, revealing potentially advantageous traits among hydrogenotrophic bacteria.Microbiome · 2025Article
- Development of a Universal Platform for the Heterologous Expression of Bidirectional [Ni-Fe]-Hydrogenases inACS synthetic biology · 2025Article
- Fully Oxidized State of the Oxygen-Tolerant [NiFe] Hydrogenase fromInorganic chemistry · 2025Article
- Probing the Influence of the Protein Scaffold on H-Cluster Reactivity via Gain-of-Function Studies─Improved HJournal of the American Chemical Society · 2025Article
- A semisynthetic, multicofactor artificial metalloenzyme retains independent site activity.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2025Article
- Characterization of the Bottlenecks and Pathways for Inhibitor Dissociation from [NiFe] Hydrogenase.Journal of chemical information and modeling · 2024Article
- Stepwise conversion of the CysChemical science · 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
- The Fully Oxidized State of the Glutamate Coordinated OJournal of the American Chemical Society · 2023Article
- Bimetallic Sites for Catalysis: From Binuclear Metal Sites to Bimetallic Nanoclusters and Nanoparticles.Chemical reviews · 2023Review
- L-amino acids affect the hydrogenase activity and growth of Ralstonia eutropha H16.AMB Express · 2023Article
- Second and Outer Coordination Sphere Effects in Nitrogenase, Hydrogenase, Formate Dehydrogenase, and CO Dehydrogenase.Chemical reviews · 2022Review
- Electrocatalytic hydrogen generation using tripod containing pyrazolylborate-based copper(ii), nickel(ii), and iron(iii) complexes loaded on a glassy carbon electrode.RSC advances · 2022Article
- 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
- How Microbes Evolved to Tolerate Oxygen.Trends in microbiology · 2021Review
13 more citing papers are in PubMed but not listed here.
Corrections and comments
- Erratum issued
Authors and funding
11 authors at 4 institutions in 2 countries.
Funding
Abstract
Hydrogenases are essential for H(2) cycling in microbial metabolism and serve as valuable blueprints for H(2)-based biotechnological applications. However, most hydrogenases are extremely oxygen sensitive and prone to inactivation by even traces of O(2). The O(2)-tolerant membrane-bound [NiFe]-hydrogenase of Ralstonia eutropha H16 is one of the few examples that can perform H(2) uptake in the presence of ambient O(2). Here we show that O(2) tolerance is crucially related to a modification of the internal electron-transfer chain. The iron-sulfur cluster proximal to the active site is surrounded by six instead of four conserved coordinating cysteines. Removal of the two additional cysteines alters the electronic structure of the proximal iron-sulfur cluster and renders the catalytic activity sensitive to O(2) as shown by physiological, biochemical, spectroscopic and electrochemical studies. The data indicate that the mechanism of O(2) tolerance relies on the reductive removal of oxygenic species guided by the unique architecture of the electron relay rather than a restricted access of O(2) to the active site.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.