Sat, 05 Jul 2008 22:57:10 BST CiteULike: neils's Devreese http://www.citeulike.org/user/neils/author/Devreese CiteULike.org en-gb Copyright © 2004-2008 citeulike.org http://www.citeulike.org/user/neils/article/2784002 <i>FEMS Microbiology Letters, Vol. 137, No. 1. (1996), pp. 95-101.</i><br /><br />Abstract The c-type cytochrome and protein profiles were compared for a number of cultures of Paracoccus denitrificans obtained from a range of culture collections. The cultures fell into two groups corresponding to the two original isolates of this bacterial species. One group, which included NCIMB 8944, ATCC 13543, ATCC 17741, ATCC 19367, Pd 1222 and DSM 413, were similar or identical to LMD 22.21. The second group, including DSM 65 and LMG 4218, were similar or identical to LMD 52.44. These groupings were not compatible with the recorded history of culture deposition. Mass spectrometry and amino acid sequence comparisons showed that the cytochrome c-550 of the LMD 52.44 culture group differed by 16% from that of the LMD 22.21 group, and yet was only 1% different from the cytochrome c-550 of Thiosphaera pantotropha. These results suggest that consideration should be given to creation of a new species of Paracoccus pantotropha, which would include Thiosphaera pantotropha and Paracoccus denitrificans LMD 52.44. The cytochromes c-550 of Paracoccus denitrificans and Thiosphaera pantotropha: a need for re-evaluation of the history of Paracoccus cultures Celia Goodhew Graham Pettigrew Bart Devreese Jozef Beeumen Rob Spanning Simon Baker Neil Saunders Stuart Ferguson Ian Thompson FEMS Microbiology Letters, Vol. 137, No. 1. (1996), pp. 95-101. 2008-05-11T09:37:08-00:00 1996 FEMS Microbiology Letters 137 1 95 101 analysis cytochrome paracoccus sequence http://www.citeulike.org/user/neils/article/2783972 <i>Biochemistry, Vol. 36, No. 26. (1 July 1997), pp. 7958-7966.</i><br /><br />The amino acid sequence of the diheme cytochrome c peroxidase from Paracoccus denitrificans has been determined as the result of sequence analysis of peptides generated by chemical and enzymatic cleavages of the apoprotein. The sequence shows 60% similarity to the cytochrome c peroxidase from Pseudomonas aeruginosa, 39% similarity to an open reading frame encoding a putative triheme c-type cytochrome in Escherichia coli, and remote similarity to the MauG proteins from two methylotrophic bacteria. It is proposed, on the basis of the pattern of conserved residues in the sequences, that a change in iron coordination in the N-terminal heme domain may accompany reduction to the active mixed valence state, a change which may be accompanied by conformational adjustments in the highly conserved interface between the N- and C-terminal domains. These conformational adjustments may also lead to the appearance of a second Ca2+ binding site in the mixed valence enzyme. The exposed edge of the heme in the C-terminal domain is surrounded by several different patterns of charged residues in the Paracoccus and Pseudomonas enzymes, and this is consistent with the interaction of the former with the highly positively charged front face of the donor cytochrome c-550. Structural characterization of Paracoccus denitrificans cytochrome c peroxidase and assignment of the low and high potential heme sites. W Hu G Van Driessche B Devreese CF Goodhew DF McGinnity N Saunders V Fulop GW Pettigrew JJ Van Beeumen doi:10.1021/bi963131e Biochemistry, Vol. 36, No. 26. (1 July 1997), pp. 7958-7966. 2008-05-11T09:18:21-00:00 1997 Biochemistry 0006-2960 36 26 7958 7966 calcium cytochrome haem paracoccus peroxidase potential