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[Ni]

Sellmann1, Geipel, Moll

  • 1Institut für Anorganische Chemie Universität Erlangen-Nürnberg Egerlandstrasse 1, 91058 Erlangen (Germany).

Angewandte Chemie (International Ed. in English)
|February 12, 2000
PubMed
Summary
This summary is machine-generated.

This study reveals how nickel-iron [NiFe] hydrogenases activate hydrogen (H2). A specific nickel complex with thiolate donors is shown to be sufficient for catalyzing H2 heterolysis, clarifying enzyme mechanisms.

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Area of Science:

  • Biochemistry
  • Bioinorganic Chemistry
  • Enzyme Catalysis

Background:

  • Hydrogenases are crucial enzymes for biological hydrogen and energy metabolism.
  • The precise mechanism of H2 activation by [NiFe] hydrogenases remains unclear.
  • Controversy exists regarding the oxidation states of metals involved in hydrogenase activity.

Purpose of the Study:

  • To elucidate the mechanism of H2 activation by [NiFe] hydrogenases.
  • To investigate the role of metal oxidation states in hydrogenase catalysis.
  • To demonstrate the catalytic capability of a specific nickel complex in H2 heterolysis.

Main Methods:

  • Synthesis and characterization of a novel nickel-thiolate complex.
  • Spectroscopic analysis to determine metal oxidation states and complex geometry.

Related Experiment Videos

  • Catalytic assays to evaluate H2 heterolysis activity.

    • Main Results:

    • The title complex features a distorted, diamagnetic Ni(II) center coordinated by thiolate donors.
    • This Ni(II) complex effectively catalyzes the heterolytic cleavage of H2.
    • The results provide direct evidence for the involvement of Ni(II) in the catalytic cycle.

    Conclusions:

    • A distorted diamagnetic Ni(II) center and thiolate donors are sufficient for catalyzing H2 heterolysis.
    • This finding clarifies a key step in the mechanism of [NiFe] hydrogenases.
    • The study resolves controversies surrounding metal oxidation states in hydrogenase function.