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Related Experiment Videos

Structure-function relationships among the nickel-containing hydrogenases.

A E Przybyla1, J Robbins, N Menon

  • 1Department of Biochemistry, University of Georgia, Athens 30602.

FEMS Microbiology Reviews
|February 11, 1992
PubMed
Summary
This summary is machine-generated.

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Nickel-containing hydrogenases share a common large subunit gene, crucial for nickel binding. This conserved gene structure is key to understanding the diversity and function of these important enzymes.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • Nickel-containing hydrogenases are diverse enzymes crucial for energy metabolism.
  • Understanding their structure and function is vital for biotechnological applications.

Purpose of the Study:

  • To summarize and discuss the enzymology of various nickel-containing hydrogenases.
  • To investigate the subunit localization of nickel and iron-sulfur clusters.
  • To propose conserved structural motifs responsible for nickel ligation.

Main Methods:

  • Comparative analysis of hydrogenase operons and genes.
  • Sequence analysis of large subunit genes, focusing on conserved motifs.
  • Review and discussion of Extended X-ray Absorption Fine Structure (EXAFS) and Electron Paramagnetic Resonance (EPR) spectroscopy data.

Related Experiment Videos

  • Site-directed mutagenesis of the (NiFe) hydrogenase-1 gene from Escherichia coli.

    • Main Results:

    • A common large subunit gene is the sole conserved feature across all nickel-containing hydrogenases, uniting them into a diverse gene family.
    • Conserved amino acid motifs (R-X-C-X-X-C and D-P-C-X-X-C) in the large subunit are proposed to ligate the active site nickel.
    • Biochemical, molecular, and biophysical data support proposed nickel ligand environments in different redox states.

    Conclusions:

    • The large subunit gene is a unifying feature of nickel-containing hydrogenases, indicating a shared evolutionary origin.
    • Conserved amino acid sequences in the large subunit are critical for nickel coordination.
    • Detailed understanding of nickel environments in hydrogenases can be achieved through integrated biochemical and biophysical approaches.