Paracoccus versutus

Electron transfer, 36 341-342 Capeillire-Blandin model, 36 283-284 centers, XAS, 36 322-323 chin, of Paracoccus versutus, 45 351-401 correlated pairs... 

Paracoccus denitrificans, 45 352 respiratory chain, 45 353-362 Paracoccus versutus, electron transfer chain, 45 351-401 Paraelement defined, 28 169... 

Cua centers exist in two redox states [Cu(II)Cu(I)] and [Cu(I)Cu(I)]. The oxidized species is a fully delocalized mixed-valence pair (formally two Cu+ 1.5 ions), as revealed by EPR spectroscopy (Kroneck et al., 1988, 1990). Despite the similar coordination geometry around copper, these systems display sharper NMR lines than do the BCP due to a shorter electron relaxation time of the paramagnetic center (wlO "s) (dementi and Luchinat, 1998). NMR studies are available for the native Cua centers from the soluble fragments of the The. thermophilus, Paracoc-cus denitrificans, Paracoccus versutus, and Bacillus subtilis oxidases (Bertini et al., 1996 Dennison et al., 1995 Luchinat et al., 1997 Salgado et al., 1998a) and Pseudomonas stutzeri N2O reductase (Holz et al., 1999), as well as for engineered Cua sites in amicyanin (Dennison et al., 1997) and Escherichia coli quinol oxidase (Kolczak et al., 1999). 

Cytochrome aa3-type oxidase of thiobacilli has been highly purified from Aci-dithiobacillus ferrooxidans (Kai et al., 1992) besides the oxidase from S. novella as described below. Although Paracoccus versutus has cytochrome aa3-type oxidase, it has not yet been purified (Kelly, 1989). Cytochrome cbb3-type cytochrome c oxidase has been obtained from Thiobacillus sp. W5 which resembles T. 

A. The Respiratory Network of Paracoccus versutus and Paracoccus denitrificans... 

Complete Amino Acid Sequences of Amicyanins from Paracoccus versutus and Parococcus denitrificans ... 

Comparison of Amino Acid Sequences of Cytochrome C550 from Paracoccus versutus AND Paracoccus denitrificans°... 

Groups 9 and 10. Paramagnetic NMR for cobalt-substituted amicyanin shows that the methionine side-chain residue interacts less strongly with the metal in Paracoccus denitrificans amicyanin than in the P. versutus variant.1215 The i I NMR spectra of Co(P), where P = dodeca-substituted porphyrins, show (dxz,dyz)4(dxy)1 electron configurations.1216 The paramagnetic 111 NMR spectrum of the cobalt(II) derivative of spinach plastocyanin has been completely assigned.1217... 

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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