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Gene Review

Rru_A0362  -  cytochrome c1

Rhodospirillum rubrum ATCC 11170

 
 
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Disease relevance of Rru_A0362

 

High impact information on Rru_A0362

  • Formation of selenodiglutathione was paralleled by a rapid reduction of cytochrome c, a known oxidant for superoxide anions [5].
  • There is no sequence similarity to mitochondrial cytochrome c, except at the heme binding site [1].
  • The three-dimensional structure of this loop replacement mutant RepA2 cytochrome c, and a second mutant RepA2(Val 20) cytochrome c in which residue 20 was back substituted to valine, were determined using X-ray diffraction techniques [6].
  • Binding of mitochondrial cytochrome c but not of mitochondrial cytochrome c2 is strongly inhibited by low concentrations of poly-L-lysine [7].
  • Electrostatic effects on the kinetics of electron transfer reactions of cytochrome c caused by binding to negatively charged lipid bilayer vesicles [8].
 

Chemical compound and disease context of Rru_A0362

 

Biological context of Rru_A0362

  • Comparison of the N-terminal protein sequences with the protein sequences deduced from the nucleotide sequence showed that only cytochrome c1 is processed during transport and assembly of the three subunits of the complex [10].
 

Anatomical context of Rru_A0362

  • In Ch. minutissimum chromatophores that retained their endogenous cytochrome c pool, one more electrogenic phase was revealed (tau = 20 microseconds) [11].
  • Difference absorption spectra of Rps. rutila membranes indicate that there is not tetraheme reaction center cytochrome c, such as is characteristic of Rps. viridis [12].
 

Associations of Rru_A0362 with chemical compounds

  • The reduction of cobalt phenanthroline and ferricyanide by bound cytochrome c proceeded by nonexponential kinetics, as compared with the monophasic kinetics observed in the absence of vesicles [8].
  • From the results obtained, it appears that in both organisms: a) ubiquinone functions as an electron carrier between the cytochromes, and b) both antimycin A and DBMIB inhibit cyclic electron flow in the segment...cytochrome b leads to ubiquinone leads to cytochrome c..., but at different sites [13].
  • These liposomes exhibit respiratory control and are able to couple electron transfer from quinol to cytochrome c to proton translocation across the liposome membrane in a manner consistent with a Q-cycle mechanism [14].
  • During illumination, the azido-Q becomes covalently attached to the cytochrome b peptide and, to a lesser extent, to cytochrome c1 [15].
  • The amino-acid composition of Pa. denitrificans cytochrome c' showed the high alanine and low proline content characteristic of the group and reflecting the predominantly alpha-helical character of the protein [4].
 

Analytical, diagnostic and therapeutic context of Rru_A0362

  • Near-infrared magnetic circular dichroism of cytochrome c' [16].
  • The cytochrome c' was purified from the latter using the device of sequential molecular exclusion chromatography in the dimeric and monomeric states [4].
  • The possibility of axial ligation of cytochrome c1 by the amino terminus of the polypeptide was also assessed by acetylating the N-terminus of Rb. capsulatus cytochrome c1 and comparing the properties of the acetylated and unmodified samples [17].

References

  1. Amino acid sequence of cytochrome c' from the purple photosynthetic bacterium Rhodospirillum rubrum S1. Meyer, T.E., Ambler, R.P., Bartsch, R.G., Kamen, M.D. J. Biol. Chem. (1975) [Pubmed]
  2. Basis for monomer stabilization in Rhodopseudomonas palustris cytochrome c' derived from the crystal structure. Shibata, N., Iba, S., Misaki, S., Meyer, T.E., Bartsch, R.G., Cusanovich, M.A., Morimoto, Y., Higuchi, Y., Yasuoka, N. J. Mol. Biol. (1998) [Pubmed]
  3. The amino acid sequence of cytochrome c' from the purple sulphur bacterium Chromatium vinosum. Ambler, R.P., Daniel, M., Meyer, T.E., Bartsch, R.G., Kamen, M.D. Biochem. J. (1979) [Pubmed]
  4. Cytochrome c' of Paracoccus denitrificans. Gilmour, R., Goodhew, C.F., Pettigrew, G.W. Biochim. Biophys. Acta (1991) [Pubmed]
  5. Similarities between the abiotic reduction of selenite with glutathione and the dissimilatory reaction mediated by Rhodospirillum rubrum and Escherichia coli. Kessi, J., Hanselmann, K.W. J. Biol. Chem. (2004) [Pubmed]
  6. The structure and function of omega loop A replacements in cytochrome c. Murphy, M.E., Fetrow, J.S., Burton, R.E., Brayer, G.D. Protein Sci. (1993) [Pubmed]
  7. Interaction of horse cytochrome c with the photosynthetic reaction center of Rhodospirillum rubrum. Bosshard, H.R., Snozzi, M., Bachofen, R. J. Bioenerg. Biomembr. (1987) [Pubmed]
  8. Electrostatic effects on the kinetics of electron transfer reactions of cytochrome c caused by binding to negatively charged lipid bilayer vesicles. Cheddar, G., Tollin, G. Arch. Biochem. Biophys. (1991) [Pubmed]
  9. Oxidation of cytochrome c2 and of cytochrome c by reaction centers of Rhodospirillum rubrum and Rhodobacter sphaeroides. The effect of ionic strength and of lysine modification on oxidation rates. van der Wal, H.N., van Grondelle, R., Millett, F., Knaff, D.B. Biochim. Biophys. Acta (1987) [Pubmed]
  10. The pet genes of Rhodospirillum rubrum: cloning and sequencing of the genes for the cytochrome bc1-complex. Majewski, C., Trebst, A. Mol. Gen. Genet. (1990) [Pubmed]
  11. Fast stages of photoelectric processes in biological membranes. III. Bacterial photosynthetic redox system. Drachev, L.A., Semenov AYu, n.u.l.l., Skulachev, V.P., Smirnova, I.A., Chamorovsky, S.K., Kononenko, A.A., Rubin, A.B., Uspenskaya NYa, n.u.l.l. Eur. J. Biochem. (1981) [Pubmed]
  12. Electron transfer proteins of the purple phototrophic bacterium, Rhodopseudomonas rutila. Meyer, T.E., Fitch, J., Van Driessche, G., Van Beeumen, J., Fischer, U., Bartsch, R.G., Cusanovich, M.A. Arch. Biochem. Biophys. (1991) [Pubmed]
  13. A comparison of electron transport and photophosphorylation systems of Rhodopseudomonas capsulata and Rhodospirillum rubrum. Effects of antimycin A and dibromothymoquinone. Gromet-Elhanan, Z., Gest, H. Arch. Microbiol. (1978) [Pubmed]
  14. The Rhodospirillum rubrum cytochrome bc1 complex: redox properties, inhibitor sensitivity and proton pumping. Güner, S., Robertson, D.E., Yu, L., Qiu, Z.H., Yu, C.A., Knaff, D.B. Biochim. Biophys. Acta (1991) [Pubmed]
  15. The Rhodospirillum rubrum cytochrome bc1 complex: peptide composition, prosthetic group content and quinone binding. Kriauciunas, A., Yu, L., Yu, C.A., Wynn, R.M., Knaff, D.B. Biochim. Biophys. Acta (1989) [Pubmed]
  16. Near-infrared magnetic circular dichroism of cytochrome c'. Rawlings, J., Stephens, P.J., Nafie, L.A., Kamen, M.D. Biochemistry (1977) [Pubmed]
  17. Axial heme ligation in the cytochrome bc1 complexes of mitochondrial and photosynthetic membranes. A near-infrared magnetic circular dichroism and electron paramagnetic resonance study. Finnegan, M.G., Knaff, D.B., Qin, H., Gray, K.A., Daldal, F., Yu, L., Yu, C.A., Kleis-San Francisco, S., Johnson, M.K. Biochim. Biophys. Acta (1996) [Pubmed]
 
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