Amino acid sequence of cytochrome c' from the purple photosynthetic bacterium Rhodospirillum rubrum S1.

نویسندگان

  • T E Meyer
  • R P Ambler
  • R G Bartsch
  • M D Kamen
چکیده

The amino acid sequence of cytochrome c' from the purple photosynthetic bacterium Rhodospirillum rubrum S1 has been determined and is consistent with homology to cytochrome c' from the nonphotosynthetic bacterium Alcaligenes sp. NCIB 11015. There is 29% identity in the chosen alignment of these two proteins. R. rubrum cytochrome c' is composed of a single peptide chain of 126 amino acid residues with a single heme covalently bound near the COOH terminus. There is no sequence similarity to mitochondrial cytochrome c, except at the heme binding site.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Amino Acid Sequence of Cytochrome c’ from the Purple Photosynthetic Bacterium Rhodospirillum rubrum Sl*

The amino acid sequence of cytochrome c’ from the purple photosynthetic bacterium Rhodospirillum rubrum Sl has been determined and is consistent with homology to cytochrome c’ from the nonphotosynthetic bacterium Alcaligenes sp. NCIB 11015. There is 29% identity in the chosen alignment of these two proteins. R. rubrum cytochrome c’ is composed of a single peptide chain of 126 amino acid residue...

متن کامل

N-terminal methylation of the core light-harvesting complex in purple photosynthetic bacteria.

Several core light-harvesting complexes from both sulfur and non-sulfur purple photosynthetic bacteria have been identified to be methylated at the N-terminal alpha-amino group of beta-polypeptides by using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry and nuclear magnetic resonance. Monomethylation has been confirmed for the N-terminal alanine residues of the bet...

متن کامل

Primary structure of a high potential, four-iron-sulfur ferredoxin from the photosynthetic bacterium Rhodospirillum tenue.

The amino acid sequence of a high oxidation-reduction potential iron-sulfur protein (HiPIP) isolated from the purple photosynthetic bacterium Rhodospirillum tenue has been determined. This is the smallest of the HiPIP's, containing 63 residues, with only 3 residues apparently conserved in addition to the 4 cluster-binding cysteines. A minimum of four internal genetic gaps is postulated to align...

متن کامل

Isolation and properties of two soluble heme proteins in extracts of the photoanaerobe Chromatium.

The involvement of heme proteins in photometabolism, first suggested by Hill (1, 2), seems certain from results of recent enzyme studies (3-5) and observations on systems in viva using differential spectrophotometry (6-10). Of the many heme proteins which exist in intimate association with the photoactive pigments in the functional subcellular structures of photosynthetic tissues, only three ha...

متن کامل

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.

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 ...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • The Journal of biological chemistry

دوره 250 21  شماره 

صفحات  -

تاریخ انتشار 1975