Quinol and cytochrome oxidases in the cyanobacterium Synechocystis sp. PCC 6803.

The genome of Synechocystis sp. PCC 6803 contains three sets of genes for terminal respiratory oxidases: the previously identified cytochrome aa3-type cytochrome c oxidase (CtaI), a second putative oxidase (CtaII) that we interpret to be a cytochrome bo-type quinol oxidase, and a putative cytochrome bd quinol oxidase (Cyd). Genes for the two putative oxidases were cloned, and deletion constructs were made. Strains that lack one, two, or all three of the oxidases were generated. Deletion of the respiratory oxidases had no effect on photoautotrophic or photomixotrophic growth. Strains that lack one oxidase respire at near-wild-type rates, whereas those that lack both CtaI and Cyd do not respire. Thus, CtaII does not play a significant role in cellular metabolism under the conditions tested. An expression construct containing cydAB from Synechocystis sp. PCC 6803 was able to restore aerobic growth in a strain of Escherichia coli that lacks the cytochrome bo oxidase and the cytochrome bd oxidase encoded by cydAB. These results show that the cydAB operon from Synechocystis sp. PCC 6803 encodes a functional quinol oxidase. Deletion of Cyd and/or CtaII in strains lacking photosystem I did not change the fluorescence decay kinetics after illumination, and therefore, these oxidases do not significantly utilize reducing equivalents in the thylakoid membrane. This, combined with our inability to delete CtaI from strains lacking photosystem I, suggests that CtaI is the major oxidase on the thylakoid membrane and that Cyd is localized mostly on the cytoplasmic membrane. Transcripts for ctaDI were detected under all growth conditions tested, while transcripts for cydA and ctaEII could only be detected in cells grown at low light intensity (5 microE m(-2) s(-1)).