Abstract
The homeostasis of the pyridine nucleotide pool [NAD(P)H and NAD(P)?] is maintained in Rhodobacter sphaeroides mutant strains defective in the cytochrome bc1 complex or the cytochrome c oxidases in terms of its concentration and redox state. Aerobic derepression of the puf operon, which is under the control of the PrrBA two-component system, in the CBB3 mutant strain of R. sphaeroides was shown to be not the result of changes in the redox state of the pyridine nucleotides and the ubiquinone/ ubiquinol pool. Using the bc₁ complex knock-out mutant strain of R. sphaeroides, we clearly demonstrated that the inhibitory effect of cbb₃ oxidase on spectral complex formation is not caused indirectly by the redox change of the ubiquinone/ubiquinol pool.
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