A comparison of the redox potentials of cytochrome c3 from Desulfovibrio vulgaris Hildenborough with those from Desulfovibrio vulgaris Miyazaki F effects of amino acid substitutions on the redox potentials

1997 ◽  
Vol 438 (1-2) ◽  
pp. 231-236 ◽  
Author(s):  
Jang-Su Park ◽  
Tomoaki Ohmura ◽  
Akira Katayama ◽  
Masataka Sagara ◽  
Katsumi Niki ◽  
...  
1993 ◽  
Vol 294 (3) ◽  
pp. 909-915 ◽  
Author(s):  
M A Piçarra-Pereira ◽  
D L Turner ◽  
J LeGall ◽  
A V Xavier

Several aromatic amino acid residues and haem resonances in the fully reduced form of Desulfovibrio gigas cytochrome c3 are assigned, using two-dimensional 1H n.m.r., on the basis of the interactions between the protons of the aromatic amino acids and the haem protons as well as the intrahaem distances known from the X-ray structure [Kissinger (1989) Ph.D. Thesis, Washington State University]. The interhaem interactions observed in the n.m.r. spectra are in full agreement with the D. gigas X-ray structure and also with the n.m.r. data from Desulfovibrio vulgaris (Hildenborough) [Turner, Salgueiro, LeGall and Xavier (1992) Eur. J. Biochem. 210, 931-936]. The good correlation between the calculated ring-current shifts and the observed chemical shifts strongly supports the present assignments. Observation of the two-dimensional nuclear-Overhauser-enhancement spectra of the protein in the reduced, intermediate and fully oxidized stages led to the ordering of the haems in terms of their midpoint redox potentials and their identification in the X-ray structure. The first haem to oxidize is haem I, followed by haems II, III and IV, numbered according to the Cys ligand positions in the amino acid sequences [Mathews (1985) Prog. Biophys. Mol. Biol. 54, 1-56]. Although the haem core architecture is the same for the different Desulfovibrio cytochromes c3, the order of redox potentials is different.


1988 ◽  
Vol 249 (1-2) ◽  
pp. 241-252 ◽  
Author(s):  
Pierre Bianco ◽  
Abdelhakim Manjaoui ◽  
Jean Haladjian ◽  
Mireille Bruschi

1993 ◽  
Vol 39 (4) ◽  
pp. 402-411
Author(s):  
Deborah Y. Kwoh ◽  
Thomas S. Vedvick ◽  
Ann F. McCue ◽  
Diane Gevertz

Polymerase chain reaction amplification was used to compare different regions of the cytochrome c3 gene from nine strains of Desulfovibrio vulgaris, to examine homology within the species. Six 30-base polymerase chain reaction primers and three probes were synthesized on the basis of the published nucleic acid sequence of the cytochrome c3 gene from D. vulgaris, NCIMB 8303. Amplifications were performed on genomic DNA isolated from NCIMB 8303 as well as eight other strains. Six strains, NCIMB 8302, 8305, 8306, 8311, 11779, and DSM 2119, showed amplification products of equal size and quantity to those of strain 8303. Two other strains, NCIMB 8456 and DSM 1744, either showed reduced levels or no detectable amplification products. These results were confirmed by hybridization of amplified DNA to radiolabeled probes specific for each product. DNA sequencing of a 145-bp polymerase chain reaction fragment from strains NCIMB 8302, 8303, 11779, and DSM 2119 revealed complete sequence homology between these strains, whereas slight differences were seen with strain NCIMB 8456. Amino acid sequencing of the first 20 residues of cytochrome c3 purified from strains NCIMB 8456 and 8303 also showed differences in the two proteins. In contrast to the results obtained with strain NCIMB 8456, limited homology was observed between the first 20 amino acid residues of cytochrome c3 from strain DSM 1744 and strain NCIMB 8303.Key words: cytochrome c3, Desulfovibrio, polymerase chain reaction amplification, taxonomy.


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