The primary structure of cytochrome c-554 from the green photosynthetic bacterium Chloroflexus aurantiacus

Biochemistry ◽  
1991 ◽  
Vol 30 (48) ◽  
pp. 11451-11458 ◽  
Author(s):  
Stella Dracheva ◽  
JoAnn C. Williams ◽  
Gonzalez Van Driessche ◽  
Jozef J. Van Beeumen ◽  
Robert E. Blankenship
Keyword(s):  
Cytochrome C ◽  
Primary Structure ◽  
Photosynthetic Bacterium ◽  
Chloroflexus Aurantiacus

scholarly journals Properties of a cytochrome c-enriched light particulate fraction isolated from the photosynthetic bacterium Rhodopseudomonas spheroides

1978 ◽  
Vol 174 (1) ◽  
pp. 267-275 ◽  
Author(s):  
J Barrett ◽  
C N Hunter ◽  
O T G Jones
Keyword(s):  
Cytochrome C ◽  
Sodium Dodecyl ◽  
Photosynthetic Bacterium ◽  
Particulate Fraction ◽  
Cytochrome C Reductase ◽  
Cytochrome C2 ◽  
Succinate Cytochrome C Reductase ◽  
Bulk Membrane ◽  
Nadh Cytochrome ◽  
Rhodopseudomonas Spheroides

Differential centrifugation of suspensions of French-press-disrupted Rhodopseudomonas spheroides yielded a light particulate fraction that was different in many properties from the bulk membrane fraction. It was enriched in cytochrome c and had a low cytochrome b content. When prepared from photosynthetically grown cells this fraction had a very low specific bacteriochlorophyll content. The cytochrome c of the light particles differed in absorption maxima at 77K from cytochrome c2 attached to membranes; there was pronounced splitting of the alpha-band, as is found in cytochrome c2 free in solution. Potentiometric titration at A552–A540 showed the presence of two components that fitted an n = 1 titration; one component had a midpoint redox potential of +345mV, like cytochrome c2 in solution, and the second had E0′ at pH 7.0 of +110 mV, and they were present in a ratio of approx. 2:3. Difference spectroscopy at 77K showed that the spectra of the two components were very similar. More of a CO-binding component was present in particles from photosynthetically grown cells. Light membranes purified by centrifugation on gradients of 5–60% (w/w) sucrose retained the two c cytochromes; they contained no detectable succinate-cytochrome c reductase or bacteriochlorophyll and very little ubiquinone, but they contained NADH-cytochrome c reductase and some phosphate. Electrophoresis on sodium dodecyl sulphate/polyacrylamide gels showed that the light membranes of aerobically and photosynthetically grown cells were very similar and differed greatly from other membrane fractions of R. spheroides.

Reaction Center Components of the Green Photosynthetic Bacterium Chloroflexus Aurantiacus

1984 ◽  
pp. 185-188 ◽  
Author(s):  
Henk Vasmel ◽  
Ron F. Meiburg ◽  
Herman J. M. Kramer ◽  
Hubert J. den Blanken ◽  
Leo J. de Vos ◽  
...  
Keyword(s):  
Reaction Center ◽  
Photosynthetic Bacterium ◽  
Chloroflexus Aurantiacus

scholarly journals The primary structure of Pseudomonas cytochrome c peroxidase

FEBS Letters ◽  
1989 ◽  
Vol 250 (2) ◽  
pp. 175-178 ◽  
Author(s):  
Marjaana Rönnberg ◽  
Nisse Kalkkinen ◽  
Nils Ellfolk
Keyword(s):  
Cytochrome C ◽  
Primary Structure ◽  
Cytochrome C Peroxidase

scholarly journals The amino acid sequence of cytochrome c′ from Alcaligenes sp. N.C.I.B. 11015

1973 ◽  
Vol 135 (4) ◽  
pp. 751-758 ◽  
Author(s):  
R. P. Ambler
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Amino Acid Sequence ◽  
Attachment Site ◽  
Photosynthetic Bacterium ◽  
Chromatium Vinosum ◽  
British Library ◽  
Pseudomonas Denitrificans ◽  
Single Polypeptide Chain ◽  
C Terminus

The amino acid sequence of the cytochrome c′ from Alcaligenes sp. N.C.I.B. 11015 (Iwasaki's ‘Pseudomonas denitrificans’) has been determined. This organism is the only non-photosynthetic bacterium in which the protein has been found. The protein consists of a single polypeptide chain of 127 residues, with a single haem covalently attached to two cysteines. Unlike normal cytochromes c, the haem attachment site is very close to the C-terminus. The amino acid sequence around the haem attachment site is very similar to that of Chromatium vinosum D cytochrome c′. Detailed evidence for the amino acid sequence of the protein has been deposited as Supplementary Publication SUP 50022 at the British Library (Lending Division), (formerly the National Lending Library for Science and Technology), Boston Spa, Yorks. LS23 7BQ, U.K., from whom copies may be obtained on the terms given in Biochem. J. (1973) 131, 5.

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