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A New Cytochrome C Reducing Dipeptide

Overview
Publisher Elsevier
Specialty General Medicine
Date 1990 Feb 1
PMID 2154586
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Abstract

Using absorption spectroscopy, it has been found that tyrosylphenylalanine specifically reduces cytochrome C. This effect is pH and concentration dependent with the EC +/- SE = 4.42 x 10(-3) M. At 10(-2) 2 M, tyrosylphenylalanine caused reduction which was 50% complete. The same amino acids linked together in reverse order as phenylalanyltyrosine produced only a minimal effect. Tyrosine and phenylalanine alone, serylphenylalanine, formylphenylalanine, tyrosyllysine, and tyrosylarginine did not reduce cytochrome C. Comparison of tyrosylphenylalanine to tyrosylalanine and tyrosyltyrosine showed that the phenyl group is essential to reduction. This approach may illuminate some of the unanswered questions of the chemiosmotic theory of mitochondrial energy production.

References
1.
Yu C, Yu L, King T . Kinetics of electron transfer between cardiac cytochrome c 1 and c. J Biol Chem. 1973; 248(2):528-33. View

2.
Grimes C, Piszkiewicz D, Fleischer E . Electron transfer reactions in biological systems: the reduction of ferricytochrome c by chromous ions. Proc Natl Acad Sci U S A. 1974; 71(4):1408-12. PMC: 388238. DOI: 10.1073/pnas.71.4.1408. View

3.
Romisch J, Tropschug M, Sebald W, Weiss H . The primary structure of cytochrome c1 from Neurospora crassa. Eur J Biochem. 1987; 164(1):111-5. DOI: 10.1111/j.1432-1033.1987.tb11000.x. View

4.
Chiang Y, Kaminsky L, King T . A complex of cardiac cytochrome c1 and cytochrome c. J Biol Chem. 1976; 251(1):29-36. View

5.
Kaminsky L, Chiang Y, Yu C, King T . Fluorescence studies of cytochrome c1 and a cytochrome c1-cytochrome c complex. Biochem Biophys Res Commun. 1974; 59(2):688-92. DOI: 10.1016/s0006-291x(74)80034-3. View