Role of the Tat Transport System in Nitrous Oxide Reductase Translocation and Cytochrome cd1 Biosynthesis in Pseudomonas stutzeri

摘要: By transforming N2O to N2, the multicopper enzyme nitrous oxide reductase provides a periplasmic electron sink for respiratory chain that is part of denitrification. The signal sequence carries heptameric twin-arginine consensus motif characteristic Tat pathway. We have identified tat genes Pseudomonas stutzeri and functionally analyzed unlinked tatC tatE loci. A mutant retained in cytoplasm unprocessed form lacking metal cofactors. This contrary viewing system as specific only fully assembled proteins. C618V exchange transfer center CuA rendered largely incompetent transport. location mutation C-terminal domain implies acts on completely synthesized protein sensitive late structural variation folding. generating reductase-overproducing strain, we show function TatE translocation. Further, found Sec pathways cooperate produce functional nitrite system. cytochrome cd1 was periplasm mutant, suggesting export by pathway; however, lacked heme D1 macrocycle. NirD complex required synthesis or processing putative peptide. Since NO reduction also inhibited translocation necessary multiple ways establishing anaerobic