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Cytoplasmic hydrogenase

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Official Full Name
Cytoplasmic hydrogenase
Background
The [NiFe] hydrogenases contain a minimum of two subunits known as the small (S) and large (L) subunits. The small subunit contains three iron-sulfur clusters while the large subunit contains the active site, a nickel-iron center which is connected to the solvent by a molecular tunnel. To date, periplasmic, cytoplasmic, and membrane-bound hydrogenases have been found. [NiFe] hydrogenases are known to be deactivated by molecular oxygen (O2). The [NiFe] hydrogenase of Pyrococcus furiosus is heterotetrameric wherein the additional two subunits allow the enzyme to use NAD(P)(H) as an electron carrier.
Synonyms
Cytoplasmic [NiFe]-Hydrogenase; OE-SHI; Cytoplasmic Hydrogenase; NiFe-type cytoplasmic hydrogenase; SHI; [NiFe] hydrogenase; NADP-specific NiFe-type cytoplasmic hydrogenase
Catalog Product Name EC No. CAS No. Source Price
NATE-1691 NiFe-type cytoplasmic hydrogenase from Pyrococcus furiosus, recombinant Pyrococcus furi... Inquiry

Related Reading

Cytoplasmic hydrogenase is an enzyme that plays a critical role in various metabolic processes, most notably in the utilization of hydrogen gas. This review aims to provide a detailed overview of cytoplasmic hydrogenase, including its structure, functions, clinical significance, and other relevant information. Cytoplasmic hydrogenase belongs to the family of iron-sulfur-containing (Fe-S) cluster proteins found in a wide range of microorganisms, including bacteria and archaea. This enzyme is involved in the conversion of molecular hydrogen (H2) into protons (H+) and electrons (e^-) in redox reactions. The electrons produced by cytoplasmic hydrogenases can be further utilized in various metabolic pathways, contributing to energy conservation and cellular processes.

Structure

Cytoplasmic hydrogenase from different microorganisms has a complex and varied structure. Typically, it consists of two subunits: a small subunit containing the iron-sulfur cluster binding motif and a large subunit containing the catalytic center. The active site of cytoplasmic hydrogenases usually contains iron-sulfur clusters, artificial motifs, and cofactors, such as ferredoxin and flavin adenine dinucleotide (FAD), which are essential for the catalytic activity of the hydrogenase.

Functions

  • Hydrogen Utilization: Cytoplasmic hydrogenase promotes hydrogen oxidation and is the main enzyme for hydrogen utilization in many microorganisms. This process is critical for anaerobic microorganisms because it enables microorganisms to produce ATP and maintain redox homeostasis under low oxygen conditions.
  • Conservation of Energy: The electrons generated during hydroxylation can be used to drive cellular processes such as ATP synthesis and reduction of other electron acceptors such as NAD+ and FAD.
  • Redox Homeostasis: Cytoplasmic hydrogenases contribute to the maintenance of the cellular redox state by participating in redox reactions, especially in anaerobic environments.
  • Hydrogen production: Some microorganisms possess reversible hydrogenases that are capable of producing hydrogen under certain conditions. This ability is of particular interest for potential applications in biofuel production and renewable energy.

Clinical Significance

  • Environmental bioremediation: The potential role of cytoplasmic hydrogenases in microbial bioremediation has been explored. Certain microorganisms containing this enzyme can utilize hydrogen as an electron donor to help detoxify and degrade various environmental pollutants.
  • Hydrogenase Inhibition for Antimicrobial Therapy: The development of selective inhibitors targeting cytoplasmic hydrogenases promises to be an antimicrobial therapy strategy. By disrupting the energy metabolism of specific microorganisms, hydrogenase inhibitors have the potential to inhibit microbial growth and survival.
  • Biomarkers for Hydrogen-Based Diagnostics: Measurement of hydrogenase activity in clinical samples has been proposed as a diagnostic tool for certain diseases, such as small intestinal bacterial overgrowth. Elevated hydrogen levels in exhaled breath may indicate an overgrowth of hydrogen-producing microorganisms in the gastrointestinal tract, allowing for early detection and monitoring of such conditions.

Current Research and Future Perspectives

Current research on cytoplasmic hydrogenases is focused on elucidating the molecular mechanisms underlying their catalytic activity, exploring their potential in biofuel production, and developing therapeutic strategies based on hydrogenase inhibition. The integration of hydrogenases with other metabolic pathways is also of interest as it provides opportunities for metabolic engineering and the creation of novel microbial strains with enhanced capabilities.

Conclusion

Cytoplasmic hydrogenase is an interesting enzyme involved in hydrogen utilization and various metabolic processes in microorganisms. Its structural diversity, function, and clinical significance have made it the subject of extensive research and exploration. Increased knowledge of cytoplasmic hydrogenases not only contributes to a fundamental understanding of microbial physiology, but also promises applications in biotechnology, environmental remediation, and medical diagnostics.