scholarly journals Molecular cloning, sequencing and expression of cytochrome c2 from Rhodospirillum rubrum

1990 ◽  
Vol 265 (2) ◽  
pp. 599-604 ◽  
Author(s):  
S J Self ◽  
C N Hunter ◽  
R J Leatherbarrow
Keyword(s):  
Rhodospirillum Rubrum ◽  
Signal Sequence ◽  
Photosynthetic Electron Transport ◽  
Photosynthetic Bacterium ◽  
Cytochrome Bc1 Complex ◽  
Cytochrome C2 ◽  
Mobile Electron ◽  
Purple Photosynthetic Bacterium ◽  
Sequencing And Expression ◽  
Synthetic Oligonucleotides

Cytochrome c2 (Mr 12,840) of the purple photosynthetic bacterium Rhodospirillum rubrum functions as a mobile electron carrier in the cyclic photosynthetic electron-transport system of this organism. It acts as the electron donor to photochemically oxidized reaction centres and is reduced in turn by electrons from the cytochrome bc1 complex. By using synthetic oligonucleotides based on the known amino acid sequence of the protein, the structural gene (cycA) has been identified and isolated. DNA sequence analysis indicates the presence of a typical prokaryotic 23-residue signal sequence, suggesting that the protein is synthesized as a precursor which is processed during its secretion into the periplasm. Evidence is presented for the production of assembled cytochrome c2 in Escherichia coli, but recombinants grow poorly and are unstable, suggesting toxicity of the gene product in this organism.

scholarly journals Polarization angle dependence of stark absorption spectra of spirilloxanthin bound to the reconstituted LH1 complexes using LH1-subunits isolated from the purple photosynthetic bacterium Rhodospirillum rubrum.

2012 ◽  
Vol 59 (1) ◽  
Author(s):  
Tomoko Horibe ◽  
Katsunori Nakagawa ◽  
Toshiyuki Kusumoto ◽  
Ritsuko Fujii ◽  
Richard J Cogdell ◽  
...  
Keyword(s):  
Dipole Moment ◽  
Absorption Spectra ◽  
Rhodospirillum Rubrum ◽  
Photosynthetic Bacterium ◽  
Transition Dipole Moment ◽  
Polarization Angle ◽  
Transition Dipole ◽  
Angle Dependence ◽  
Induced Dipole ◽  
Purple Photosynthetic Bacterium

Reconstituted LH1 complexes were prepared using the LH1 subunit-type complexes, isolated from the purple photosynthetic bacterium Rhodospirillum (Rs.) rubrum, and purified all-trans spirilloxanthin. Stark absorption spectra of spirilloxanthin bound to both the native and reconstituted LH1 complexes were compared in different polarization angles (χ) against the external electric field. From the polarization angle dependence of the Stark absorption spectra, two angles were determined in reference to the direction of transition dipole moment (m) of spirilloxanthin: one is the change in polarizability upon photoexcitation (Δα), θ(Δα) and the other is the change in static dipole moment upon photoexcitation (Δμ), θ(Δμ). Despite the symmetric molecular structure of all-trans spirilloxanthin, its Stark absorption spectra show pronounced values of Δμ. This large Δμ values essentially caused by the effect of induced dipole moment through Δα both in the cases for native and reconstituted LH1 complexes. However, slightly different values of θ(Δα) and θ(Δμ) observed for the native LH1 complex suggest that spirilloxanthin is asymmetrically distorted when bound to the native LH1 complex and gives rise to intrinsic Δμ value.

Binding site on Rhodospirillum rubrum cytochrome c2 for the Rhodospirillum rubrum cytochrome bc1 complex

Biochemistry ◽  
1987 ◽  
Vol 26 (24) ◽  
pp. 7688-7693 ◽  
Author(s):  
Hans Rudolf Bosshard ◽  
R. Max Wynn ◽  
David B. Knaff
Keyword(s):  
Binding Site ◽  
Rhodospirillum Rubrum ◽  
Cytochrome Bc1 ◽  
Bc1 Complex ◽  
Cytochrome Bc1 Complex ◽  
Cytochrome C2
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