A ferredoxin-dependent dihydropyrimidine dehydrogenase in Clostridium chromiireducens

Feifei Wang, Yifeng Wei, Qiang Lu, Ee Lui Ang, Huimin Zhao, Yan Zhang

Research output: Contribution to journalArticlepeer-review


Dihydropyrimidine dehydrogenase (PydA) catalyzes the first step of the reductive pyrimidine degradation (Pyd) pathway in bacteria and eukaryotes, enabling pyrimidines to be utilized as substrates for growth. PydA homologs studied to date catalyze the reduction of uracil to dihydrouracil, coupled to the oxidation of NAD(P)H. Uracil reduction occurs at a flavin mononucleotide (FMN) site, and NAD(P)H oxidation occurs at a flavin adenine dinucleotide (FAD) site, with two ferredoxin domains thought to mediate inter-site electron transfer. Here, we report the biochemical characterization of a Clostridial PydA homolog (PydAc) from a Pyd gene cluster in the strict anaerobic bacterium Clostridium chromiireducens. PydAc lacks the FAD domain, and instead is able to catalyze uracil reduction using reduced methyl viologen or reduced ferredoxin as the electron source. Homologs of PydAc are present in Pyd gene clusters in many strict anaerobic bacteria, which use reduced ferredoxin as an intermediate in their energy metabolism.

Original languageEnglish (US)
Article numberBSR20201642
JournalBioscience Reports
Issue number7
StatePublished - Jul 2020

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


Dive into the research topics of 'A ferredoxin-dependent dihydropyrimidine dehydrogenase in Clostridium chromiireducens'. Together they form a unique fingerprint.

Cite this