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Probing the ferredoxin:hydrogenase electron transfer complex by infrared difference spectroscopy.

Selmihan Sahin1,2, Johanna Brazard3, Kilian Zuchan1

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This summary is machine-generated.

Ferredoxins facilitate multi-electron redox reactions through sequential one-electron transfers. This study reveals how ferredoxins and hydrogenases interact, enabling efficient electron transfer for biological processes.

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Area of Science:

  • Biochemistry
  • Bioenergetics
  • Protein-protein interactions

Background:

  • Ferredoxins are crucial electron carriers in biological redox reactions.
  • The mechanism by which ferredoxins facilitate multi-electron transfers remains poorly understood.
  • Understanding these mechanisms is vital for fields like photosynthesis and hydrogen metabolism.

Purpose of the Study:

  • To investigate the electron transfer complexes between clostridial ferredoxin (CpFd) and [FeFe]-hydrogenases.
  • To elucidate the role of ferredoxin structure and redox state in modulating protein-protein interactions (PPIs).
  • To propose a model for efficient multi-electron transfer mediated by ferredoxins.

Main Methods:

  • Utilized Fourier-transform infrared (FTIR) spectroscopy with a non-canonical amino acid to probe electric field changes.
  • Employed in situ FTIR difference spectroscopy to observe protein structural changes upon reduction.
  • Applied microscale thermophoresis to quantify ferredoxin-hydrogenase binding affinities.

Main Results:

  • Introduced a non-canonical amino acid in CpFd to quantify electric field changes via vibrational Stark effect.
  • Observed protein structural changes and quantified redox-dependent PPIs between ferredoxin and hydrogenase.
  • Demonstrated that ferredoxin-hydrogenase affinity is modulated by the redox state of the ferredoxin.

Conclusions:

  • Ferredoxins facilitate multi-electron redox chemistry through a series of one-electron transfer events.
  • Redox-dependent PPIs play a critical role in the efficiency of electron transfer.
  • The findings provide a mechanistic model for ferredoxin-mediated multi-electron transfer.