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.
MeSH Terms
Amino Acid Sequence
Animals
Cytochrome c Group/chemical synthesis,metabolism
Electron Transport Complex IV/metabolism
Horses
Kinetics
Oxidation-Reduction
Peptide Fragments/chemical synthesis
Structure-Activity Relationship
Chemicals
Cytochrome c Group
Peptide Fragments
Electron Transport Complex IV
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
ten Kortenaar P B
Adams P J
Tesser G I
References (10)
10 references, click to expand
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