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TitleUnderstanding the Catalytic Determinant role of Diaphorase-Like Subunit in Formate Dehydrogenases via Redox Couples.
Journal, issue, pagesAdv Sci (Weinh), Page e75764, Year 2026
Publish dateMay 19, 2026
AuthorsKuncheng Zhang / Weisong Liu / Hao Su / Huijuan Cui / Yuanming Wang / Zhiguang Zhu / Chun You / Lingling Zhang /
PubMed AbstractMulti-subunit formate dehydrogenases (FDHs), which catalyze the interconversion of formate and carbon dioxide (CO), have drawn increasing attention for mitigating climate change and advancing ...Multi-subunit formate dehydrogenases (FDHs), which catalyze the interconversion of formate and carbon dioxide (CO), have drawn increasing attention for mitigating climate change and advancing environmental protection owing to their advantages of oxygen tolerance and easy heterogenous expression. However, differently sourced multi-subunit FDHs exhibit distinct catalytic biases, and the reasons remain unclear. On the basis of the exceptional observation of Rhodobacter aestuarii FDH favoring CO reduction, this study unveiled an oxidation inhibition effect in exclusively NADH/NAD-involved catalysis via kinetics analysis in terms of different redox couples. Substrate truncation positioned Fdhβ as the predominant subunit. Further studies based on structural and electrochemical insights interpreted that the slow desorption of NADH is the underlying determinant for the apparent catalytic bias. Knowledge-based rational design helped obtain a beneficial variant, RaFDH β E260Y, with a 10-fold increased catalytic activity in CO reduction, highlighting its potential for CO biotransformation and applications in low-carbon biomanufacturing. Eventually, bioinformatic analysis suggested that the diaphorase-like subunits and the catalysis regulation mechanism may widely exist in living organisms for modulating the redox balance of oxidoreductases, providing new insights into metabolism and catabolism.
External linksAdv Sci (Weinh) / PubMed:42154453
MethodsEM (single particle)
Resolution2.9 Å
Structure data

66342

9wxb

EMDB-66342, PDB-9wxb:
Cryo-EM structure of reduced form of formatedehydrogenase from Rhodobacter aestuarii (RaFDH) with NADH
Method: EM (single particle) / Resolution: 2.9 Å

Chemicals

ChemComp-FES:
FE2/S2 (INORGANIC) CLUSTER

ChemComp-MGD:
2-AMINO-5,6-DIMERCAPTO-7-METHYL-3,7,8A,9-TETRAHYDRO-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-4-ONE GUANOSINE DINUCLEOTIDE

ChemComp-6MO:
Unknown entry

ChemComp-SF4:
IRON/SULFUR CLUSTER

ChemComp-NAD:
NICOTINAMIDE-ADENINE-DINUCLEOTIDE / NAD*YM

ChemComp-FMN:
FLAVIN MONONUCLEOTIDE

Source
  • rhodobacter aestuarii (bacteria)
KeywordsOXIDOREDUCTASE / formate dehydrogenase / formate oxidation / carbon dioxide redcution / FMN / NAD

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