Paracoccus pantotrophus

The aerobic degradation of L-cysteate by Paracoccus pantotrophus is carried out by deamination to 3-sulfolactate from which sulfite is lost with the formation of pyruvate (Cook et al. 2006). The activity of the lyase (3-L-sulfolactatesulfolyase) has been shown to involve pyridoxal 5 -phosphate, and the enzyme has been found in a number of organisms using L-cysteate either as a source of carbon or as an electron acceptor (Denger et al. 2006). 

Rainey FR, Kelly DP, Stackebrandt E, et al. 1999. A re-evaluation of the taxonomy of Paracoccus denitrificans and a proposal for the combination Paracoccus pantotrophus comb. nov. Int J Syst Bacteriol 49 645-51. 

A new representative of a multicopper cluster in a protein is Cuz in nitrous oxide reductase. As was discussed above this enzyme contains a binuclear CuA centre as in COX. While the latter in addition has CuB in the form of a copper-heme group, N20 reductase has Cuz which is the site of dinitrogen formation from the substrate N20. Recently a central inorganic sulfide has been found as a ligand to copper and multiple forms of Cuz were detected in the enzyme from Paracoccus pantotrophus.134 More recently a tetranuclear copper cluster with X-S bridges was proposed as structure for Cuz..135... 

Echalier A, Goodhew CF, Pettigrew GW et al (2006) Activation and catalysis of the di-heme cytochrome c peroxidase from Paracoccus pantotrophus. Structure 14 107-117... 

Figure 4-12. Catalytic voltammetry of Paracoccus pantotrophus nitrate reductase (NarGH) adsorbed as a film on a PGE electrode at pH 6. (A) Increasing the electrode rotation rate from 0 to 3000 rpm removes the mass transport limitation of the catalytic response in 50 pM NO3 . (B) The enzyme s greater rate of chlorate reduction compared to nitrate reduction is reflected in greater distortion of the waveform through dispersion of sluggish interfacial electron transfer rates (see also Fig. 4-4C). Scan rate 10 mV s. Adapted from ref. 64. with permission.

Quentmeier A, Kraft R, Kostka S, Klockenkamper R, Friedrich CG (2000) Characterization of a new type of sulfite dehydrogenase from Paracoccus pantotrophus GB17. Arch Microbiol 175 117-125... 

Allen, J.W.A., N.J. Watmough, and S.J. Ferguson (2000). A switch in heme axial ligation prepares Paracoccus pantotrophus cytochrome cd for catalysis. Nat. Struct. Biol. 7, 885-888. 

George, S.J., J.W.A. AUen, S.J. Ferguson, and R.N.F. Thorneley (2000). Time-resolved infrared spectroscopy reveals a stable ferric heme-NO intermediate in the reaction of Paracoccus pantotrophus cytochrome cdi nitrite reductase with nitrite. /. Biol. Chem. 275, 33231-33237. 

As selected examples of more recently developed ketone reductions with recombinant whole cells following the concept of substrate-coupled in situ cofactor recycling, the work by the Schmid and Buehler group with a recombinant ADH from Thermus sp. [88] and by the Kroutil group with a DMSO-tolerant recombinant ADH from Paracoccus pantotrophus [89] shall be mentioned here. This recombinant whole-cell... 

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