• We are sorry, but NCBI web applications do not support your browser and may not function properly. More information
Logo of pnasPNASInfo for AuthorsSubscriptionsAboutThis Article
Proc Natl Acad Sci U S A. Dec 1985; 82(24): 8279–8283.
PMCID: PMC390897

Semisynthesis of horse heart cytochrome c analogues from two or three fragments.

Abstract

Horse heart cytochrome c was cleaved with cyanogen bromide. The largest fragment, [Hse65]cytochrome c-(1-65)-pentahexacontapeptide lactone, was used in condensations involving four analogues of the complementary cytochrome c-(66-104)-nonatriacontapeptide. Two of the latter compounds were obtained from a semisynthesis starting with a partially protected fragment N epsilon 86-88,99,100-penta(methylsulfonylethyloxycarbonyl)cytochrome c-(81-104)-tetracosapeptide (also arising from a cyanogen bromide-mediated degradation) and analogues of the middle part, cytochrome c-(66-80)-pentadecapeptide, which were prepared by organochemical synthesis. Two other analogues of the cytochrome c-(66-104)-nonatriacontapeptide were prepared entirely by organochemical synthesis. Each of the covalently recombined analogous cytochromes c could retain an electron in the presence of oxygen and transfer it to cytochrome c oxidase, although with different reaction rates and Michaelis constants. Their redox potentials varied over a broad range. The exchanges Tyr67----Phe(F) and Thr78----Val gave rise to analogues with a lower redox potential than native cytochrome c, while the exchange Phe82----Leu or Tyr97----Leu led to analogues with the same and a higher redox potential, respectively.

Full text

Full text is available as a scanned copy of the original print version. Get a printable copy (PDF file) of the complete article (994K), or click on a page image below to browse page by page. Links to PubMed are also available for Selected References.

Images in this article

Click on the image to see a larger version.

Selected References

These references are in PubMed. This may not be the complete list of references from this article.
  • Takano T, Dickerson RE. Conformation change of cytochrome c. I. Ferrocytochrome c structure refined at 1.5 A resolution. J Mol Biol. 1981 Nov 25;153(1):79–94. [PubMed]
  • Takano T, Dickerson RE. Conformation change of cytochrome c. II. Ferricytochrome c refinement at 1.8 A and comparison with the ferrocytochrome structure. J Mol Biol. 1981 Nov 25;153(1):95–115. [PubMed]
  • Poulos TL, Kraut J. A hypothetical model of the cytochrome c peroxidase . cytochrome c electron transfer complex. J Biol Chem. 1980 Nov 10;255(21):10322–10330. [PubMed]
  • Boon PJ, Tesser GI, Nivard RJ. Semisynthetic horse heart [65-homoserine]cytochrome c from three fragments. Proc Natl Acad Sci U S A. 1979 Jan;76(1):61–65. [PMC free article] [PubMed]
  • Tesser GI, Balvert-Geers IC. The methylsulfonylethyloxycarbonyl group, a new and versatile amino protective function. Int J Pept Protein Res. 1975;7(4):295–305. [PubMed]
  • Corradin G, Harbury HA. Reconstitution of horse heart cytochrome c: reformation of the peptide bond linking residues 65 and 66. Biochem Biophys Res Commun. 1974 Dec 23;61(4):1400–1406. [PubMed]
  • Boon PJ, Tesser GI. Protection and deprotection of horse cytochrome c. Int J Pept Protein Res. 1985 May;25(5):510–516. [PubMed]
  • Tesser GI, Adams PJ, Ten Kortenaar PB, Boots HA. Reproducibility of gel-chromatography. Int J Pept Protein Res. 1984 Aug;24(2):192–194. [PubMed]
  • Ferguson-Miller S, Brautigan DL, Margoliash E. Correlation of the kinetics of electron transfer activity of various eukaryotic cytochromes c with binding to mitochondrial cytochrome c oxidase. J Biol Chem. 1976 Feb 25;251(4):1104–1115. [PubMed]
  • Boon PJ, Van Raay AJ, Tesser GI, Nivard RJ. Semisynthesis, conformation and cytochrome c oxidase activity of eight cytochrome c analogues. FEBS Lett. 1979 Dec 1;108(1):131–135. [PubMed]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

Formats:

Related citations in PubMed

See reviews...See all...

Cited by other articles in PMC

See all...

Links

  • PubMed
    PubMed
    PubMed citations for these articles
  • Substance
    Substance
    PubChem Substance links

Recent Activity

Your browsing activity is empty.

Activity recording is turned off.

Turn recording back on

See more...