ArticleThe Journal of biological chemistry2012
Genetic analysis of the Hox hydrogenase in the cyanobacterium Synechocystis sp. PCC 6803 reveals subunit roles in association, assembly, maturation, and function.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 48 citations in OpenAlex.
- Removal of Photosystem I Subunit PsaE Leads to Photosynthetic Hydrogen Production in a Cyanobacterial PsaF-HoxYH Fusion Strain.Plant, cell & environment · 2026Article
- Increased hydrogen and ethanol production in transformants of the filamentous cyanobacterium Phormidium lacuna.Archives of microbiology · 2026Article
- Comparative study of phycoerythrobilin synthases for fine-tuning photosynthetic light-harvesting complexes, phycobilisomes.Scientific reports · 2026Article
- Article
- Reactivation and long-term stabilization of the [NiFe] Hox hydrogenase of Synechocystis sp. PCC6803 by glutathione after oxygen exposure.The Journal of biological chemistry · 2025Article
- Gallionellaceae pangenomic analysis reveals insight into phylogeny, metabolic flexibility, and iron oxidation mechanisms.mSystems · 2023Article
- Article
- The structure and reactivity of the HoxEFU complex from the cyanobacteriumThe Journal of biological chemistry · 2020Article
- Metabolic Potential for Reductive Acetogenesis and a Novel Energy-Converting [NiFe] Hydrogenase inFrontiers in microbiology · 2020Article
- Metalloproteins in the Biology of Heterocysts.Life (Basel, Switzerland) · 2019Review
- Novel prosthecate bacteria from the candidate phylum Acetothermia.The ISME journal · 2018Article
- Article
- Perturbation of formate pathway and NADH pathway acting on the biohydrogen production.Scientific reports · 2017Article
- A tight tunable range for Ni(II) sensing and buffering in cells.Nature chemical biology · 2017Article
- Computational metabolic engineering strategies for growth-coupled biofuel production byMetabolic engineering communications · 2016Article
- Type II Toxin-Antitoxin Systems in the Unicellular Cyanobacterium Synechocystis sp. PCC 6803.Toxins · 2016Article
- [NiFe]-hydrogenase is essential for cyanobacterium Synechocystis sp. PCC 6803 aerobic growth in the dark.Scientific reports · 2015Article
- Cyanobacterial hydrogenases and hydrogen metabolism revisited: recent progress and future prospects.International journal of molecular sciences · 2015Review
- Metals in cyanobacteria: analysis of the copper, nickel, cobalt and arsenic homeostasis mechanisms.Life (Basel, Switzerland) · 2014Review
- Advances in the function and regulation of hydrogenase in the cyanobacterium Synechocystis PCC6803.International journal of molecular sciences · 2014Review
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hydrogenases are metalloenzymes that catalyze 2H(+) + 2e(-) ↔ H(2). A multisubunit, bidirectional [NiFe]-hydrogenase has been identified and characterized in a number of bacteria, including cyanobacteria, where it is hypothesized to function as an electron valve, balancing reductant in the cell. In cyanobacteria, this Hox hydrogenase consists of five proteins in two functional moieties: a hydrogenase moiety (HoxYH) with homology to heterodimeric [NiFe]-hydrogenases and a diaphorase moiety (HoxEFU) with homology to NuoEFG of respiratory Complex I, linking NAD(P)H ↔ NAD(P)(+) as a source/sink for electrons. Here, we present an extensive study of Hox hydrogenase in the cyanobacterium Synechocystis sp. PCC 6803. We identify the presence of HoxEFUYH, HoxFUYH, HoxEFU, HoxFU, and HoxYH subcomplexes as well as association of the immature, unprocessed large subunit (HoxH) with other Hox subunits and unidentified factors, providing a basis for understanding Hox maturation and assembly. The analysis of mutants containing individual and combined hox gene deletions in a common parental strain reveals apparent alterations in subunit abundance and highlights an essential role for HoxF and HoxU in complex/subcomplex association. In addition, analysis of individual and combined hox mutant phenotypes in a single strain background provides a clear view of the function of each subunit in hydrogenase activity and presents evidence that its physiological function is more complicated than previously reported, with no outward defects apparent in growth or photosynthesis under various growth conditions.
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