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Structural Insights Into CO2 Transport Pathways in a W-Formate Dehydrogenase: Structural Basis for CO2 Reduction.

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Molybdenum/Tungsten-dependent formate dehydrogenases (Fdhs) show a CO2-specific pathway. A novel retention site enhances CO2 reduction efficiency by concentrating substrates near the active site.

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Area of Science:

  • Biocatalysis
  • Enzyme mechanisms
  • Structural biology

Background:

  • Molybdenum/Tungsten-dependent formate dehydrogenases (Fdhs) are crucial biocatalysts for CO2 capture and conversion.
  • Previous research suggested two substrate-access tunnels in Fdhs, but CO2-specific pathways lacked experimental validation.

Purpose of the Study:

  • To investigate the substrate-access pathways and identify CO2-specific routes in Nitratidesulfovibrio vulgaris FdhAB.
  • To elucidate the role of a potential substrate-retention site in CO2 reduction efficiency.

Main Methods:

  • Crystallography with gas pressurization (Kr, O2, CO2)
  • Molecular dynamics simulations
  • Site-directed mutagenesis
  • Enzyme kinetics assays

Main Results:

  • A substrate-retention site was identified, consistently occupied by small molecules in crystal structures.
  • CO2 and H2O utilize a novel side branch tunnel in addition to the main tunnel to reach the retention site.
  • The retention site enhances CO2 reduction by increasing local substrate concentration, improving catalytic efficiency.
  • Mutations affecting the retention site selectively impaired CO2 reduction but not formate oxidation.

Conclusions:

  • Experimental evidence confirms a CO2-specific pathway in FdhAB.
  • The identified retention site plays a key role in efficient CO2 reduction.
  • Structural determinants for enhanced CO2 reduction by Fdhs have been uncovered.