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Investigating the Molybdenum Nitrogenase Mechanistic Cycle Using Spectroelectrochemistry.

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Researchers studied molybdenum nitrogenase (MoFe) using electrochemistry and spectroscopy. They observed key protonation events in the enzyme's active site, advancing understanding of nitrogen fixation.

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Area of Science:

  • Biochemistry
  • Bioinorganic Chemistry
  • Electrochemistry

Background:

  • Molybdenum nitrogenase is vital for biological nitrogen fixation, converting N2 to NH3.
  • The precise catalytic mechanisms, including electron and proton transfer, are not fully understood.

Purpose of the Study:

  • To investigate the catalytic mechanism of molybdenum nitrogenase using a biohybrid electrochemical system.
  • To elucidate the role of specific amino acid residues and intermediates in nitrogenase catalysis.

Main Methods:

  • Covalent attachment of molybdenum nitrogenase (MoFe) to gold electrodes.
  • Utilizing surface-enhanced infrared absorption spectroscopy (SEIRA) coupled with electrochemistry.
  • Performing quantum mechanics/molecular mechanics (QM/MM) calculations.

Main Results:

  • Observed terminal and bridging S-H stretching frequencies during nitrogenase turnover, indicating protonation of bridging sulfides in FeMoco.
  • Provided direct experimental evidence for the role of these protonated sulfides in catalysis.
  • Investigated CO inhibition, revealing CO binding and unbinding dynamics under electrochemical conditions.

Conclusions:

  • The study provides novel insights into the mechanistic cycle of molybdenum nitrogenase.
  • Established a foundation for studying other nitrogenases, such as vanadium and iron nitrogenases.
  • Demonstrated the utility of biohybrid electrochemical systems for mechanistic studies of metalloenzymes.