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• SO4483-SO4485 are induced by nitrate, TMAO, and
  DMSO relative to fumarate (Beliaev 2005) and by
  uranium (Bencheikh-Latmani 2005) suggesting a
  possible protective role in anaerobic respiratory
  processes.
• Mutants lacking SO1427 and CymA are unable to
  grow on DMSO. However, the cluster of genes
  encoding these genes is induced by thiosulfate
  and not DMSO suggesting that a different
  sulfur-containing substrate may be a more
  favorable e- acceptor. A second DMSO-like
  cluster is also present, but conditions that
  promote its expression have yet to be defined.
  Note that the predicted localization of the
  terminal reductases are lipoproteins are hence
  may be involved in electron transfer to insoluble
  sulfur-containing materials.
• The cytochrome bc1 complex transfers electrons
  from ubiquinol to the cbb3-type cytochrome
  oxidase. Mutants lacking SO0610 are defective in
  reduction of MnO2 and chromate.
• Fumarate reduction is abolished in the FccA
  mutant demonstrating that this periplasmic
  localized protein is the sole fumarate reductase.
  The CymA mutant is also unable to grow on
  fumarate as expected.
• Mutants lacking SO0479 are deficient in manganese
  oxide reduction. This novel cytochrome has its
  own cytochrome assembly proteins. This locus is
  adjacent to a Nos-like copper transporter
  suggesting that one or more members of this
  complex contain a copper center.
• The cbb3-type cytochrome oxidase complex is used
  under conditions of low oxygen tension.
  Mutations in CcoO (SO2363) result in reduced
  growth on both TMAO and nitrate suggesting that
  this complex is necessary for removal of residual
  oxygen during respiration of these substrates.
• ScyA (SO0264) is proposed to be the donor to the
  cbb3-type cytochrome oxidase because it is the
  only abundant high potential soluble cytochrome
  under aerobic conditions (Meyer 2004).

• Beliaev, A.S., et. al., J. Bacteriol. 2005.
  187(20)7138-7145.
• Bencheikh-Latmani, R., et. al., Appl. Environ.
  Microbiol. 2005.
• 71(11)7453-7460.
• Hedderich, R., et. al., FEMS Microbiol Rev. 1999.
  22353381.
• Marietou A, et. al., FEMS Microbiol Lett. 2005.
  248(2)217-225.
• Meyer, T.E., et. al., OMICS. 2004. 8(1)57-77.
• Mowat, C.G.,et. al., Nat. Struct. Mol. Biol.
  2004. 11(10)1023-1024
• Schwalb, C., et. al., Biochem. 2003.
  42(31)9491-9497.