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Alkenes undergo reduction by the addition of molecular hydrogen to give alkanes. Because the process generally occurs in the presence of a transition-metal catalyst, the reaction is called catalytic hydrogenation.
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Catalytic hydrogenation of alkenes is a transition-metal catalyzed reduction of the double bond using molecular hydrogen to give alkanes. The mode of hydrogen addition follows syn stereochemistry.
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Hydrogen bonds are weak attractions between atoms that have formed other chemical bonds. One of these atoms is electronegative, like oxygen, and has a partial negative charge. The other is a hydrogen atom that has bonded with another electronegative atom and has a partial positive charge.
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A hydrogen bond is formed when a weakly positive hydrogen atom already bonded to one electronegative atom (for example, the oxygen in the water molecule) is attracted to another electronegative atom from another polar molecule, such as water (H2O), hydrogen fluoride (HF), or ammonia (NH3). The huge electronegativity difference between the H atom (2.1) and the atom to which it is bonded (4.0 for an F atom, 3.5 for an O atom, or 3.0 for an N atom), combined with the very small size of an H atom...
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A safety cap protects hydrogenase from oxygen attack.

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  • 1Photobiotechnology, Department of Plant Biochemistry, Ruhr-Universität Bochum, 44801, Bochum, Germany.

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Summary

[FeFe]-hydrogenases are efficient H2 catalysts. A novel protein morphing mechanism involving a cysteine safety cap protects the H-cluster cofactor from oxygen inactivation, enabling reversible transitions between active and inactive states.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • [FeFe]-hydrogenases are crucial for H2 production but are inactivated by oxygen.
  • The catalytic cofactor, H-cluster, is sensitive to dioxygen, leading to irreversible damage.

Purpose of the Study:

  • To elucidate the mechanism of reversible oxygen-induced inactivation in [FeFe]-hydrogenase CbA5H.
  • To identify the structural elements responsible for protecting the H-cluster from oxygen.

Main Methods:

  • X-ray crystallography
  • Rational protein design
  • Direct electrochemistry
  • Fourier-transform infrared spectroscopy

Main Results:

  • A protein morphing mechanism controls the transition between the active H_ox and inactive H_inact states.
  • A conserved cysteine residue acts as a safety cap, coordinating the substrate-binding site and preventing O2 access.
  • This protection is remotely controlled by three non-conserved amino acids distant from the H-cluster.

Conclusions:

  • A novel remote-controlled mechanism protects the [FeFe]-hydrogenase H-cluster from oxygen inactivation.
  • Protein structure modifications can be engineered to enhance enzyme stability and reversibility.
  • Understanding this mechanism is key for developing robust hydrogenase biocatalysts.