d.c. polarograms of bovine heart cytochrome c show reduction currents at low potentials. This is observed in buffer solutions with pH values between 1 and 10.5. These currents are attributed to catalytic hydrogen formation (pre-sodium currents). After succinylation of the protein, the current in glycine-NaOH buffer of pH 10.5 disappears almost completely, whereas that in acetate buffer of pH 4.5 is affected only slightly. It is concluded that different groups are responsible for the currents observed in these two buffer
Abstract-The dependence of formal potential (F”) on temperature for cytochrome c in phosphate buffer...
Cytochromes belong to a diverse family of heme-containing redox proteins that function as intermedia...
AbstractThe cytochrome c oxidase activity of the bovine heart enzyme decreases substantially at alka...
d.c. polarograms of bovine heart cytochrome c show reduction currents at low potentials. This is obs...
The effects of the ionic atmosphere on the enthalpic and entropic contributions to the reduction pot...
This paper reports on a pulse polarographic study of low-potential electron-transferring proteins at...
Investigation of the redox thermodynamics of horse heart cytochrome c at bare glassy carbon electrod...
The changes in reduction potential of cytochrome c from bovine heart were factorized into the enthal...
Bovine heart cytochrome c (cyt c) was studied through cyclic voltammetry, H-1 NMR and circular dichr...
T he alkaline isomerizat ion of horse heart cytochrome c and ligandbinding cyt c in the pres ence of...
In recent years, the enormous increase in high-resolution three-dimensional structures of proteins t...
Cyclic voltammetry experiments were carried out on native Saccharomyces cerevisiae iso-1-cytochrome ...
The range of salts used as supporting electrolytes in electrochemical studies of redox proteins and ...
AbstractThe kinetics of the formation and relaxation of transmembrane electric potential (Δψ) during...
The redox potential of horse and bovine heart cytochromes c determined through cyclic voltammetry is...
Abstract-The dependence of formal potential (F”) on temperature for cytochrome c in phosphate buffer...
Cytochromes belong to a diverse family of heme-containing redox proteins that function as intermedia...
AbstractThe cytochrome c oxidase activity of the bovine heart enzyme decreases substantially at alka...
d.c. polarograms of bovine heart cytochrome c show reduction currents at low potentials. This is obs...
The effects of the ionic atmosphere on the enthalpic and entropic contributions to the reduction pot...
This paper reports on a pulse polarographic study of low-potential electron-transferring proteins at...
Investigation of the redox thermodynamics of horse heart cytochrome c at bare glassy carbon electrod...
The changes in reduction potential of cytochrome c from bovine heart were factorized into the enthal...
Bovine heart cytochrome c (cyt c) was studied through cyclic voltammetry, H-1 NMR and circular dichr...
T he alkaline isomerizat ion of horse heart cytochrome c and ligandbinding cyt c in the pres ence of...
In recent years, the enormous increase in high-resolution three-dimensional structures of proteins t...
Cyclic voltammetry experiments were carried out on native Saccharomyces cerevisiae iso-1-cytochrome ...
The range of salts used as supporting electrolytes in electrochemical studies of redox proteins and ...
AbstractThe kinetics of the formation and relaxation of transmembrane electric potential (Δψ) during...
The redox potential of horse and bovine heart cytochromes c determined through cyclic voltammetry is...
Abstract-The dependence of formal potential (F”) on temperature for cytochrome c in phosphate buffer...
Cytochromes belong to a diverse family of heme-containing redox proteins that function as intermedia...
AbstractThe cytochrome c oxidase activity of the bovine heart enzyme decreases substantially at alka...