ArticleThe Biochemical journal2014
How the structure of the large subunit controls function in an oxygen-tolerant [NiFe]-hydrogenase.
Article in The Biochemical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 39 citations in OpenAlex.
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- Second and Outer Coordination Sphere Effects in Nitrogenase, Hydrogenase, Formate Dehydrogenase, and CO Dehydrogenase.Chemical reviews · 2022Review
- Molecular Hydrogen Metabolism: a Widespread Trait of Pathogenic Bacteria and Protists.Microbiology and molecular biology reviews : MMBR · 2020Review
- Hup-Type Hydrogenases of Purple Bacteria: Homology Modeling and Computational Assessment of Biotechnological Potential.International journal of molecular sciences · 2020Article
- Conserved Histidine Adjacent to the Proximal Cluster Tunes the Anaerobic Reductive Activation ofChemElectroChem · 2018Article
- Retuning the Catalytic Bias and Overpotential of a [NiFe]-Hydrogenase via a Single Amino Acid Exchange at the Electron Entry/Exit Site.Journal of the American Chemical Society · 2017Article
- Proton Transfer in the Catalytic Cycle of [NiFe] Hydrogenases: Insight from Vibrational Spectroscopy.ACS catalysis · 2017Review
- Identification of a stable complex between a [NiFe]-hydrogenase catalytic subunit and its maturation protease.FEBS letters · 2017Article
- Biosynthesis of Salmonella enterica [NiFe]-hydrogenase-5: probing the roles of system-specific accessory proteins.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2016Article
- Anaerobic Formate and Hydrogen Metabolism.EcoSal Plus · 2016Review
- Exploring the directionality of Escherichia coli formate hydrogenlyase: a membrane-bound enzyme capable of fixing carbon dioxide to organic acid.MicrobiologyOpen · 2016Article
- Re-engineering a NiFe hydrogenase to increase the H2 production bias while maintaining native levels of O2 tolerance.Chemical communications (Cambridge, England) · 2016Article
- How the oxygen tolerance of a [NiFe]-hydrogenase depends on quaternary structure.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2016Article
- Electrochemical insights into the mechanism of NiFe membrane-bound hydrogenases.Biochemical Society transactions · 2016Review
- Distribution of Hydrogenases in Cyanobacteria: A Phylum-Wide Genomic Survey.Frontiers in genetics · 2016Article
- Metagenomic Sequencing Unravels Gene Fragments with Phylogenetic Signatures of O2-Tolerant NiFe Membrane-Bound Hydrogenases in Lacustrine Sediment.Current microbiology · 2015Article
- What is the trigger mechanism for the reversal of electron flow in oxygen-tolerant [NiFe] hydrogenases?Chemical science · 2015Article
- Atmospheric hydrogen scavenging: from enzymes to ecosystems.Applied and environmental microbiology · 2015Review
- Host hydrogen rather than that produced by the pathogen is important for Salmonella enterica serovar Typhimurium virulence.Infection and immunity · 2015Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Salmonella enterica is an opportunistic pathogen that produces a [NiFe]-hydrogenase under aerobic conditions. In the present study, genetic engineering approaches were used to facilitate isolation of this enzyme, termed Hyd-5. The crystal structure was determined to a resolution of 3.2 Å and the hydro-genase was observed to comprise associated large and small subunits. The structure indicated that His229 from the large subunit was close to the proximal [4Fe-3S] cluster in the small subunit. In addition, His229 was observed to lie close to a buried glutamic acid (Glu73), which is conserved in oxygen-tolerant hydrogenases. His229 and Glu73 of the Hyd-5 large subunit were found to be important in both hydrogen oxidation activity and the oxygen-tolerance mechanism. Substitution of His229 or Glu73 with alanine led to a loss in the ability of Hyd-5 to oxidize hydrogen in air. Furthermore, the H229A variant was found to have lost the overpotential requirement for activity that is always observed with oxygen-tolerant [NiFe]-hydrogenases. It is possible that His229 has a role in stabilizing the super-oxidized form of the proximal cluster in the presence of oxygen, and it is proposed that Glu73could play a supporting role in fine-tuning the chemistry of His229 to enable this function.
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