Molybdenum and tungsten-dependent formate dehydrogenases

Area of Science:

• Microbiology
• Biochemistry
• Enzymology

Background:

• Prokaryotic formate metabolism is highly diverse, involving C1 pathways and energy generation.
• Formate dehydrogenase (FDH) enzymes catalyze the reversible oxidation of formate to carbon dioxide.
• FDH enzymes are crucial for various physiological roles in prokaryotes.

Purpose of the Study:

• To review the diverse physiological roles of FDH in prokaryotes.
• To highlight the structural organization and active site features of FDH enzymes.
• To discuss the mechanistic strategies employed by FDH for formate oxidation and CO2 reduction.

Main Methods:

• Literature review of prokaryotic formate metabolism and FDH enzymes.
• Analysis of structural and mechanistic studies on FDH.
• Exploration of the potential of FDH in carbon dioxide sequestration.

Main Results:

• FDH enzymes exhibit modular structures and diverse active site configurations.
• Various FDH types have evolved to fulfill distinct physiological functions.
• FDH can catalyze the reverse reaction, reducing CO2, which has implications for carbon capture.

Conclusions:

• FDH enzymes are central to prokaryotic formate metabolism, with diverse roles and structures.
• Understanding FDH mechanisms offers insights into energy conservation and C1 cycling.
• The CO2 reduction capability of FDH presents opportunities for biotechnological applications in carbon sequestration.