scholarly journals The amino acid sequence of cytochrome c3 from Desulfovibrio vulgaris. (N.C. I.B. 8303)

1968 ◽  
Vol 109 (3) ◽  
pp. 47P-48P ◽  
Author(s):  
R P Ambler
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Desulfovibrio Vulgaris ◽  
Cytochrome C3

Amino Acid Sequence of Cytochrome C3 from Desulfovibrio vulgaris, Miyazaki

1980 ◽  
Vol 87 (6) ◽  
pp. 1747-1756 ◽  
Author(s):  
Wataru SHINKAI ◽  
Toshiharu HASE ◽  
Tatsuhiko YAGI ◽  
Hiroshi MATSUBARA
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Desulfovibrio Vulgaris ◽  
Cytochrome C3

Characterization and complete amino acid sequence of ferrodoxin II from Desulfovibrio vulgaris Miyazaki

Biochimie ◽  
1988 ◽  
Vol 70 (12) ◽  
pp. 1815-1820 ◽  
Author(s):  
Naoko Okawara ◽  
Mari Ogata ◽  
Tatsuhiko Yagi ◽  
Sadao Wakabayashi ◽  
Hiroshi Matsubara
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Desulfovibrio Vulgaris ◽  
Complete Amino Acid Sequence

scholarly journals Structural studies on Desulfovibrio gigas cytochrome c3 by two-dimensional 1H-nuclear-magnetic-resonance spectroscopy

1993 ◽  
Vol 294 (3) ◽  
pp. 909-915 ◽  
Author(s):  
M A Piçarra-Pereira ◽  
D L Turner ◽  
J LeGall ◽  
A V Xavier
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequences ◽  
Reduced Form ◽  
Desulfovibrio Vulgaris ◽  
Resonance Spectroscopy ◽  
Two Dimensional ◽  
Redox Potentials ◽  
Cytochrome C3 ◽  
X Ray ◽  
Desulfovibrio Gigas

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.

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