Exemplar Abstract for Rhodopseudomonas acidophila Pfennig 1969 (Approved Lists 1980) and Rhodoblastus acidophilus (Pfennig 1969) Imhoff 2001 emend. Hördt et al. 2020.

2003 ◽  
Author(s):  
Charles Thomas Parker ◽  
Nicole Danielle Osier ◽  
George M Garrity
Keyword(s):  
Rhodopseudomonas Acidophila ◽  
Rhodoblastus Acidophilus

scholarly journals Intraband dynamics and exciton trapping in the LH2 complex of Rhodopseudomonas acidophila

2021 ◽  
Vol 154 (4) ◽  
pp. 045102
Author(s):  
Erling Thyrhaug ◽  
Marco Schröter ◽  
Eglė Bukartė ◽  
Oliver Kühn ◽  
Richard Cogdell ◽  
...  
Keyword(s):  
Rhodopseudomonas Acidophila

scholarly journals Spectroscopy on Individual Light-Harvesting 1 Complexes of Rhodopseudomonas acidophila

2002 ◽  
Vol 83 (3) ◽  
pp. 1701-1715 ◽  
Author(s):  
Martijn Ketelaars ◽  
Clemens Hofmann ◽  
Jürgen Köhler ◽  
Tina D. Howard ◽  
Richard J. Cogdell ◽  
...  
Keyword(s):  
Light Harvesting ◽  
Rhodopseudomonas Acidophila

The complete amino acid sequences of the b 800—850 antenna polypeptides from rhodopseudomonas acidophila strain 7750

1988 ◽  
Vol 43 (1-2) ◽  
pp. 77-83 ◽  
Author(s):  
Iwan Bissig ◽  
René A. Brunisholz ◽  
Franz Suter ◽  
Richard J. Cogdell ◽  
Herbert Zuber
Keyword(s):  
Amino Acids ◽  
Rhodobacter Capsulatus ◽  
Light Harvesting ◽  
Ion Exchange Resin ◽  
Amino Acid Sequences ◽  
Molar Ratio ◽  
Light Harvesting Complexes ◽  
Rhodopseudomonas Acidophila ◽  
Terminal Domain ◽  
Iodosobenzoic Acid

Spectrally pure B 800-850 light harvesting complexes of Rhodopseudomonas acidophila 7750 were prepared by chromatography of LDAO-solubilised photosynthetic membranes on Whatmann DE-52 ion exchange resin. Two low molecular mass polypeptides (α, β) have been isolated by organic solvent extraction of the lyophilised B 800-850 light harvesting complexes. Their primary structures were determined by liquid phase sequencer runs, by the sequence analyses of C-terminal o-iodosobenzoic acid fragments, by hydrazinolysis and by carboxypeptidase degradation. B 800-850-a consists of 53 amino acids and is 45.3% and 50.9% homologous to the B 800-850- a antenna polypeptides of Rhodobacter sphaeroides and Rhodobacter capsulatus, respectively. The second very short polypeptide (B800-850-β, 41 amino acids) is 61.0% and 56.1% homologous to the corresponding polypeptides of Rb. sphaeroides and Rb. capsulatus. The molar ratio of the two polypeptides is about 1:1. Both polypeptides show a hydrophilic N-terminal domain, a very hydrophobic central domain and a short C-terminal domain. In both polypeptides the typical His residues, identified in all antenna polypeptides of purple nonsulphur bacteria as possible bacteriochlorophyll binding sites, were found

Nitrogen assimilation in Rhodopseudomonas acidophila

1978 ◽  
Vol 119 (1) ◽  
pp. 1-5 ◽  
Author(s):  
R. A. Herbert ◽  
E. Siefert ◽  
N. Pfennig
Keyword(s):  
Nitrogen Assimilation ◽  
Rhodopseudomonas Acidophila

Crystallization of the B800–820 light-harvesting complex from Rhodopseudomonas acidophila strain 7750

1992 ◽  
Vol 224 (2) ◽  
pp. 527-528 ◽  
Author(s):  
N. Guthrie ◽  
G. MacDermott ◽  
R.J. Cogdell ◽  
A.A. Freer ◽  
N.W. Isaacs ◽  
...  
Keyword(s):  
Light Harvesting ◽  
Light Harvesting Complex ◽  
Rhodopseudomonas Acidophila

scholarly journals Structural aspects of the dye-linked alcohol dehydrogenase of Rhodopseudomonas acidophila

1979 ◽  
Vol 181 (3) ◽  
pp. 517-524 ◽  
Author(s):  
C W Bamforth ◽  
J R Quayle
Keyword(s):  
Alcohol Dehydrogenase ◽  
Paracoccus Denitrificans ◽  
Colorimetric Assay ◽  
Protein Band ◽  
Atomic Absorption Spectrophotometry ◽  
Biochemical Properties ◽  
Visible Absorption ◽  
Rhodopseudomonas Acidophila ◽  
Alcohol Dehydrogenase Activity ◽  
Alcohol Dehydrogenation

1. A dye-linked alcohol dehydrogenase was purified 60-fold from extracts of Rhodopseudomonas acidophila 10050 grown aerobically on ethanol. 2. The properties of this enzyme were identical with those of the alcohol dehydrogenase synthesized by this organism during growth on methanol anaerobically in the light, and they are judged to be the same enzyme. 3. The enzyme gave a single protein band, coincident with alcohol dehydrogenase activity, during electrophoresis on polyacrylamide gel. 4. The amino acid composition, ioselectric point, u.v. and visible absorption spectra of the enzyme were determined and compared with those of other similar enzymes. 5. The presence of 0.7–1.0 g-atom of non-haem, acidlabile iron/mol of enzyme was shown by atomic absorption spectrophotometry and colorimetric assay. The iron could not be dissociated from the enzyme by dialysis against chelating agents. 6. E.p.r. spectroscopy of the enzyme did not indicate any redox function for the iron during alcohol dehydrogenation, but showed a signal at g = 2.00 consistent with the presence of a protein-bound organic free radical. 8. Antisera were raised against alcohol (methanol) dehydrogenases purified from Rhodopseudomonas acidophila, Paracoccus denitrificans and Methylophilus methylotrophus. 9. The antiserum to the Rhodopseudomonas acidophila enzyme cross-reacted with neither of the two other antisera, nor with crude extracts of methanol-grown Hyphomicrobium X and Pseudomonas AM1, thus emphasizing its singular biochemical properties.

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