ArticleApplied and environmental microbiology2011
[NiFe] hydrogenase from Alteromonas macleodii with unusual stability in the presence of oxygen and high temperature.
Article in Applied and environmental microbiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 34 citations in OpenAlex.
- A Gas Chromatography-Based Workflow Leads to the Detection of Hydrogenase Activity in Native Bacteria.Chembiochem : a European journal of chemical biology · 2026Article
- Genome sequence ofMicrobiology resource announcements · 2024Article
- Photobiohydrogen Production and Strategies for HAdvances in biochemical engineering/biotechnology · 2023Article
- Heterologous Hydrogenase Overproduction Systems for Biotechnology-An Overview.International journal of molecular sciences · 2020Review
- Genomic, metabolic and phenotypic variability shapes ecological differentiation and intraspecies interactions of Alteromonas macleodii.Scientific reports · 2020Article
- Metagenomics Meets Electrochemistry: Utilizing the Huge Catalytic Potential From the Uncultured Microbial Majority for Energy-Storage.Frontiers in bioengineering and biotechnology · 2020Article
- Identification of Cultivable Bacteria from Tropical Marine Sponges and Their Biotechnological Potentials.Tropical life sciences research · 2018Article
- Novel hydrogenases from deep-sea hydrothermal vent metagenomes identified by a recently developed activity-based screen.The ISME journal · 2018Article
- Elucidating hydrogenase surfaces and tracing the intramolecular tunnels for hydrogenase inhibition in microalgal species.Bioinformation · 2016Article
- Why Close a Bacterial Genome? The Plasmid of Alteromonas Macleodii HOT1A3 is a Vector for Inter-Specific Transfer of a Flexible Genomic Island.Frontiers in microbiology · 2016Article
- Distribution of Hydrogenases in Cyanobacteria: A Phylum-Wide Genomic Survey.Frontiers in genetics · 2016Article
- Modeling three-dimensional structure of two closely related Ni-Fe hydrogenases.Photosynthesis research · 2015Article
- Cyanobacterial hydrogenases and hydrogen metabolism revisited: recent progress and future prospects.International journal of molecular sciences · 2015Review
- Designed surface residue substitutions in [NiFe] hydrogenase that improve electron transfer characteristics.International journal of molecular sciences · 2015Article
- A broad survey reveals substitution tolerance of residues ligating FeS clusters in [NiFe] hydrogenase.BMC biochemistry · 2014Article
- Dual organism design cycle reveals small subunit substitutions that improve [NiFe] hydrogenase hydrogen evolution.Journal of biological engineering · 2013Article
- Heterologous expression of Alteromonas macleodii and Thiocapsa roseopersicina [NiFe] hydrogenases in Synechococcus elongatus.PloS one · 2011Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hydrogenases are enzymes involved in the bioproduction of hydrogen, a clean alternative energy source whose combustion generates water as the only end product. In this article we identified and characterized a [NiFe] hydrogenase from the marine bacterium Alteromonas macleodii "deep ecotype" with unusual stability toward oxygen and high temperature. The A. macleodii hydrogenase (HynSL) can catalyze both H(2) evolution and H(2) uptake reactions. HynSL was expressed in A. macleodii under aerobic conditions and reached the maximum activity when the cells entered the late exponential phase. The higher level of hydrogenase activity was accompanied by a greater abundance of the HynSL protein in the late-log or stationary phase. The addition of nickel to the growth medium significantly enhanced the hydrogenase activity. Ni treatment affected the level of the protein, but not the mRNA, indicating that the effect of Ni was exerted at the posttranscriptional level. Hydrogenase activity was distributed ∼30% in the membrane fraction and ∼70% in the cytoplasmic fraction. Thus, HynSL appears to be loosely membrane-bound. Partially purified A. macleodii hydrogenase demonstrated extraordinary stability. It retained 84% of its activity after exposure to 80°C for 2 h. After exposure to air for 45 days at 4°C, it retained nearly 100% of its activity when assayed under anaerobic conditions. Its catalytic activity in the presence of O(2) was evaluated by the hydrogen-deuterium (H-D) exchange assay. In 1% O(2), 20.4% of its H-D exchange activity was retained. The great stability of HynSL makes it a potential candidate for biotechnological applications.
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