Cytochrome Paracoccus pantotrophus

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... 

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. 

Similar enzymes are known to occur in Paracoccus (Thiobacillus) versutus (Lu and Kelly, 1984a,b) and T. thioparus (Lyric and Suzuki, 1970b). The P. versutus enzyme has a molecular mass of 44 kDa and contains cytochrome c-551. The T. thioparus enzyme has one atom each of nonheme iron and molybdenum (Kessler and Rajagopalan, 1972). A membrane-bound type sulfite dehydrogenase has been obtained from Thiobacillus (Acidithiobacillus) thiooxidans JCM 7814. The enzyme has the molecular mass of 400 kDa and catalyzes the reduction of horse ferricytochrome c with sulfite (Nakamura et al., 1995, 2001). Also from Paracoccus (Thio-sphaera) pantotrophus GB17, sulfite dehydrogenase has been obtained. Its molecular mass is 190 kDa (2 x 47 kDa + 2 x 50 kDa) and it has 4 heme C molecules and 1-2 atoms of molybdenum (Quentmeier et al., 2000). Furthermore,... 

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