Biological Electron Transfer Chains: Genetics, Composition and Mode of Operation 1998
DOI: 10.1007/978-94-011-5133-7_19
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Chimeric Quinol Oxidases Expressed in Paracoccus Denitrificans

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1998
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“…Given the close relationship of the P. denitrificans quinol oxidase to its E. coli homologue, a similar spatial structure can be inferred from these results. Another indication of their structural similarity is the retention of some enzymatic activity (about 20% both in membranes and in the isolated complex compared to the native P. denitrificans quinol oxidase) after replacement of the qoxA gene coding for subunit II of the P. denitrificans enzyme by the equivalent gene, cyoA, from the bo 3 -type quinol oxidase of E. coli (324). It is not yet clear whether the chimeric quinol oxidase retains the ability to translocate one proton across the membrane per electron transferred to oxygen, as do the parent oxidases.…”
Section: Genes Of Oxygen Respirationmentioning
confidence: 99%
“…Given the close relationship of the P. denitrificans quinol oxidase to its E. coli homologue, a similar spatial structure can be inferred from these results. Another indication of their structural similarity is the retention of some enzymatic activity (about 20% both in membranes and in the isolated complex compared to the native P. denitrificans quinol oxidase) after replacement of the qoxA gene coding for subunit II of the P. denitrificans enzyme by the equivalent gene, cyoA, from the bo 3 -type quinol oxidase of E. coli (324). It is not yet clear whether the chimeric quinol oxidase retains the ability to translocate one proton across the membrane per electron transferred to oxygen, as do the parent oxidases.…”
Section: Genes Of Oxygen Respirationmentioning
confidence: 99%