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Primary Structure Characterization of a Rhodocyclus tenuis Diheme Cytochrome c Reveals the Existence of Two Different Classes of Low-Potential Diheme Cytochromes c in Purple Phototropic Bacteria

The complete amino acid sequence of a 26-kDa low redox potential cytochrome c-551 from Rhodocyclus tenuis was determined by a combination of Edman degradation and mass spectrometry. There are 240 residues including two heme binding sites at positions 41, 44, 128, and 132. There is no evidence for ge...

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Published in:Archives of biochemistry and biophysics 2000-09, Vol.381 (1), p.53-60
Main Authors: Devreese, Bart, Brigé, Ann, Backers, Katrien, Van Driessche, Gonzalez, Meyer, Terrance E, Cusanovich, Michael A, Van Beeumen, Jozef J
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description The complete amino acid sequence of a 26-kDa low redox potential cytochrome c-551 from Rhodocyclus tenuis was determined by a combination of Edman degradation and mass spectrometry. There are 240 residues including two heme binding sites at positions 41, 44, 128, and 132. There is no evidence for gene doubling. The only known homolog of Rc. tenuis cytochrome c-551 is the diheme cytochrome c-552 from Pseudomonas stutzeri which contains 268 residues and heme binding sites at nearly identical positions. There is 44% overall identity between the Rc. tenuis and Ps. stutzeri cytochromes with 10 internal insertions and deletions. The Ps. stutzeri cytochrome is part of a denitrification gene cluster, whereas Rc. tenuis is incapable of denitrification, suggesting different functional roles for the cytochromes. Histidines at positions 45 and 133 are the fifth heme ligands and conserved histidines at positions 29, 209, and 218 and conserved methionines at positions 114 and 139 are potential sixth heme ligands. There is no obvious homology to the low-potential diheme cytochromes characterized from other purple bacterial species such as Rhodobacter sphaeroides. There are therefore at least two classes of low-potential diheme cytochromes c found in phototrophic bacteria. There is no more than 11% helical secondary structure in Rc. tenuis cytochrome c-551 suggesting that there is no relationship to class I or class II c-type cytochromes.
doi_str_mv 10.1006/abbi.2000.1971
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There are 240 residues including two heme binding sites at positions 41, 44, 128, and 132. There is no evidence for gene doubling. The only known homolog of Rc. tenuis cytochrome c-551 is the diheme cytochrome c-552 from Pseudomonas stutzeri which contains 268 residues and heme binding sites at nearly identical positions. There is 44% overall identity between the Rc. tenuis and Ps. stutzeri cytochromes with 10 internal insertions and deletions. The Ps. stutzeri cytochrome is part of a denitrification gene cluster, whereas Rc. tenuis is incapable of denitrification, suggesting different functional roles for the cytochromes. Histidines at positions 45 and 133 are the fifth heme ligands and conserved histidines at positions 29, 209, and 218 and conserved methionines at positions 114 and 139 are potential sixth heme ligands. There is no obvious homology to the low-potential diheme cytochromes characterized from other purple bacterial species such as Rhodobacter sphaeroides. There are therefore at least two classes of low-potential diheme cytochromes c found in phototrophic bacteria. 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There are therefore at least two classes of low-potential diheme cytochromes c found in phototrophic bacteria. 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There are 240 residues including two heme binding sites at positions 41, 44, 128, and 132. There is no evidence for gene doubling. The only known homolog of Rc. tenuis cytochrome c-551 is the diheme cytochrome c-552 from Pseudomonas stutzeri which contains 268 residues and heme binding sites at nearly identical positions. There is 44% overall identity between the Rc. tenuis and Ps. stutzeri cytochromes with 10 internal insertions and deletions. The Ps. stutzeri cytochrome is part of a denitrification gene cluster, whereas Rc. tenuis is incapable of denitrification, suggesting different functional roles for the cytochromes. Histidines at positions 45 and 133 are the fifth heme ligands and conserved histidines at positions 29, 209, and 218 and conserved methionines at positions 114 and 139 are potential sixth heme ligands. There is no obvious homology to the low-potential diheme cytochromes characterized from other purple bacterial species such as Rhodobacter sphaeroides. There are therefore at least two classes of low-potential diheme cytochromes c found in phototrophic bacteria. There is no more than 11% helical secondary structure in Rc. tenuis cytochrome c-551 suggesting that there is no relationship to class I or class II c-type cytochromes.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>11019819</pmid><doi>10.1006/abbi.2000.1971</doi><tpages>8</tpages></addata></record>
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subjects Amino Acid Sequence
Bacterial Proteins
Betaproteobacteria - chemistry
Betaproteobacteria - genetics
Binding Sites - genetics
Conserved Sequence
Cytochrome c Group - chemistry
Cytochrome c Group - classification
Cytochrome c Group - genetics
diheme
Drug Stability
Genes, Bacterial
Heme - chemistry
Ligands
low-potential cytochrome
Mass Spectrometry
Molecular Sequence Data
Pseudomonas - chemistry
Pseudomonas - genetics
Rhodocyclus tenuis
Sequence Homology, Amino Acid
Species Specificity
title Primary Structure Characterization of a Rhodocyclus tenuis Diheme Cytochrome c Reveals the Existence of Two Different Classes of Low-Potential Diheme Cytochromes c in Purple Phototropic Bacteria
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