the FMN enzyme protoporphyrinogen IX oxidase (HemG) of Escherichia coli abstracts six electrons from its substrate and transfers them via ubiquinone, cytochrome bo3 and cytochrome bd oxidase to oxygen. Under anaerobic conditions electrons are transferred via menaquinone, fumarate and nitrate reductase. Cytochrome bo3 , cytochrome bd, and nitrate reductase contribute to the proton motive force that drives ATP formation
Escherichia coli strain SASX38 lacks functional protoporphyrinogen IX dehydrogenase activity and is reported to be deficient in HemG. Sequence analysis of the SASX38 hemG gene reveals a deletion from nucleotide 152 to 470. This results in a predicted HemG protein that remains in frame but lacks 106 internal amino acids, including the long chain insert loop
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native enzyme solubilized from membranes by anion exchange chromatography, recombinant His-tagged enzyme from Bacillus megaterium byy affinity chromatography and gel filtration. Removal of the fused His-tag via protease digestion does not change the catalytic properties