Journal ArticleDOI
Thermodynamics of the redox reaction of cytochromes c of five different species
Rimona Margalit,Abel Schejter +1 more
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The evaluation of the heat change for several cytochromes c, made by applying the Van?About:
This article is published in FEBS Letters.The article was published on 1970-02-16. It has received 54 citations till now. The article focuses on the topics: Redox.read more
Citations
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Book ChapterDOI
7 Cytochromes c
TL;DR: All cytochromes c are oxidation-reduction proteins involved in either respiration or photosynthesis, related more to the heme and its attachment to the polypeptide chain than to the protein which surrounds it.
Book ChapterDOI
New Perspectives on c-Type Cytochromes
T. E. Meyer,Martin D. Kamen +1 more
TL;DR: This chapter discusses the various classes of c-type cytochromes, primarily as they occur in nonmitochondrial systems, and their further description as subclasses based on structural relationships observed for purified proteins.
Journal ArticleDOI
Cytochrome c: a thermodynamic study of the relationships among oxidation state, ion-binding and structural parameters. 1. The effects of temperature, pH and electrostatic media on the standard redox potential of cytochrome c.
Rimona Margalit,Abel Schejter +1 more
TL;DR: The standard redox potential at I= 0.01, 25°C and pH 7.0 has been determined for the following species of cytochrome c: horse heart, baker's yeast isoenzyme-1, Candida species yeast, tuna heart and turkey heart, and the thermodynamic parameters of the redox reaction were evaluated.
Journal ArticleDOI
Guanidine hydrochloride and acid denaturation of horse, cow, and Candida krusei cytochromes c.
J. A. Knapp,C. N. Pace +1 more
Journal ArticleDOI
Spectroelectrochemical study of cytochrome c oxidase: pH and temperature dependences of the cytochrome potentials. Characterization of site-site interactions.
TL;DR: The observed absorbance changes at the alpha and Soret absorbance maxima have been used to estimate the extents of reduction of cytochromes a and a3, and indicate that the cytochrome a site participates in anticooperative thermodynamic interactions which involve all three of the other metal sites in the protein.
References
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Journal ArticleDOI
The Oxidation Potential of the System Potassium Ferrocyanide–Potassium Ferricyanide at Various Ionic Strengths
Journal ArticleDOI
Thermodynamic aspects of the potassium hexacyano-ferrate(III)-(II) system. II. Reduction potential
Journal ArticleDOI
Determination of iron in heme compounds. II. Hemoglobin and myoglobin.
TL;DR: The procedure is carried out entirely in one vessel, digestion of the protein being effected by perchloric acid-hydrogen peroxide followed by spectrophotometric determination of iron as the ferrous-o-phenanthroline complex.
Journal ArticleDOI
Thermodynamic aspects of the potassium hexacyanoferrate(III)-(II) system. I. Ion association.
Journal ArticleDOI
Physicochemical properties of bakers' yeast iso-1-cytochrome c.
Irit Aviram,Abel Schejter +1 more
TL;DR: The more favorable enthalpy and less favorable entropy changes than for the reaction with horse cytochrome c indicate that in the yeast protein the noncovalent interactions between various residues of the polypeptide chain are weaker and the molecule possesses more degrees of freedom.
Related Papers (5)
Cytochrome c: a thermodynamic study of the relationships among oxidation state, ion-binding and structural parameters. 1. The effects of temperature, pH and electrostatic media on the standard redox potential of cytochrome c.
Rimona Margalit,Abel Schejter +1 more