A Bacterial Multidomain NAD-Independent d-Lactate Dehydrogenase Utilizes Flavin Adenine Dinucleotide and Fe-S Clusters as Cofactors and Quinone as an Electron Acceptor for d-Lactate Oxidization

Supplemental material

  • Supplemental file 1 -

    Tables S1 (Purification procedure of heterologously expressed Fe-S d-iLDH), S2 (Strains and plasmids), and S3 (Oligonucleotides) and Fig. S1 (Characterization of Fe-S d-iLDH from P. putida KT2440), S2 (Expression procedure for FAD-containing dehydrogenase domain and Fe-S oxidoreductase domain), S3 (Enzymatic properties of Fe-S d-iLDH and FAD-containing dehydrogenase domain), S4 (Construction of Fe-S oxidoreductase domain variants), S5 (Time course study of growth of P. putida KT2440 and its derivatives), S6 (Sequence features of d-iLDHs and other related FAD-binding-4 proteins), and S7 (Evolutionary relationships of GlcD proteins and predicted FAD-containing dehydrogenase domains of Fe-S d-iLDHs)

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