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Bacterial cytochrome c nitrite reductase: new structural and functional aspects.

P Stach1, O Einsle, W Schumacher

  • 1Universität Konstanz, Fachbereich Biologie, Germany.

Journal of Inorganic Biochemistry
|June 1, 2000
PubMed
Summary

This study reveals that calcium ions stimulate the activity of cytochrome c nitrite reductase, a key enzyme in the nitrogen cycle. The enzyme also shows high sulfite reductase activity and a potential reaction intermediate was identified.

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Area of Science:

  • Biochemistry
  • Microbiology
  • Enzymology

Background:

  • Cytochrome c nitrite reductase is crucial for the biological nitrogen cycle, catalyzing the reduction of nitrite to ammonia.
  • The crystal structure of this pentaheme protein from Sulfurospirillum deleyianum has been determined, revealing a homodimeric structure with closely packed hemes.
  • The enzyme binds a Ca(2+) ion near its active site heme.

Purpose of the Study:

  • To investigate the structural and functional aspects of cytochrome c nitrite reductase, particularly the role of Ca(2+).
  • To explore the substrate specificity and reaction mechanism of the enzyme.
  • To identify potential reaction intermediates during nitrite reduction.

Main Methods:

  • X-ray crystallography for structural determination.

Related Experiment Videos

  • Enzyme activity assays at varying protein concentrations and in the presence/absence of Ca(2+).
  • Rapid freeze electron paramagnetic resonance (EPR) spectroscopy under turnover conditions.

    • Main Results:

    • The enzyme exists as a homodimer in solution, with activity dependent on protein concentration.
    • Calcium ions significantly stimulate enzyme activity, and their removal decreases activity.
    • The enzyme efficiently reduces nitrite, NO, hydroxylamine, and O-methyl hydroxylamine to ammonia. It also exhibits high sulfite reductase activity.
    • A paramagnetic Fe(II)-NO adduct, a potential reaction intermediate, was detected using EPR spectroscopy.

    Conclusions:

    • Calcium ions play a vital role in modulating the activity of cytochrome c nitrite reductase.
    • The enzyme possesses broad substrate specificity and participates in multiple reduction reactions.
    • The identified Fe(II)-NO adduct provides insights into the mechanism of nitrite reduction to ammonia.