Inorganic clusters with a [Fe2MoOS3] core-a functional model for acetylene reduction by nitrogenases

Area of Science:

• Bioinorganic Chemistry
• Organometallic Chemistry
• Catalysis

Background:

• Nitrogenases are crucial enzymes catalyzing nitrogen fixation.
• The iron-molybdenum cofactor (FeMoco) is the active site of nitrogenases.
• Understanding FeMoco's mechanism requires synthetic models.

Purpose of the Study:

• To synthesize the first wholly inorganic mimic of a part of the FeMoco active site.
• To investigate the reactivity of novel hydride-containing inorganic clusters.
• To elucidate the mechanism of acetylene reduction by the inorganic model.

Main Methods:

• Synthesis of dihydride and vinyl monohydride inorganic clusters.
• Characterization using spectroscopic and analytical techniques.
• Reactivity studies involving acetylene reduction.

Main Results:

• Successful synthesis and characterization of two transient hydride-containing inorganic clusters, [Fe2MoOS3]-dihydride and [Fe2MoOS3]-vinyl monohydride.
• The dihydride complex reduces acetylene to ethylene, proceeding via the vinyl monohydride complex.
• A transient low-valent complex is generated during the catalytic cycle via reductive elimination.

Conclusions:

• The inorganic clusters represent the first functional mimic of the [Fe2MoOS3] core of FeMoco.
• The study provides insights into the mechanism of nitrogenase-catalyzed reactions.
• This work opens avenues for developing new catalysts for nitrogen fixation.