@article{mbs:/content/journal/micro/10.1099/00221287-135-12-3467, author = "Santini, Claire-Lise and Karibian, Doris and Vasishta, Anil and Boxer, David and Giordano, Gerard", title = "Escherichia coli Molybdoenzymes Can Be Activated by Protein FA from Several Gram-negative Bacteria", journal= "Microbiology", year = "1989", volume = "135", number = "12", pages = "3467-3475", doi = "https://doi.org/10.1099/00221287-135-12-3467", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-135-12-3467", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", abstract = "Six Gram-negative bacteria (Klebsiella pneumoniae, Erwinia chrysanthemi, Proteus vulgaris, Serratia marescens, Salmonella typhimurium, and Pseudomonas aeruginosa) were shown to contain an FA-type protein capable of activating aponitrate reductase, apotrimethylamine N-oxide reductase and apoformate dehydrogenase of Escherichia coli. Protein FA activity was highest in Erwinia chrysanthemi and lowest in Pseudomonas aeruginosa. All the species also contained the low-M r (≤ 1500) heat-resistant material previously reported to be necessary for the protein-FA-dependent activation of E. coli chlB nitrate reductase.", }