TY - JOUR
T1 - Cytochrome c
T2 - A Thermodynamic Study of the Relationship among Oxidation State, Ion‐Binding and Structural Parameters Cation Binding to Horse‐Heart Ferrocytochrome c
AU - MARGALIT, Rimona
AU - SCHEJTER, Abel
PY - 1974/7
Y1 - 1974/7
N2 - The specific binding of cations to horse heart ferrocytochrome c has been studied, using the gel filtration method. The cations investigated were: Mg2+, Co2+, cinchonine and proflavine. The stability constants are in the range of 5–8 mM−1, and the number of binding sites per protein molecule are 1 to 2. The temperature dependence of the stability constant for the Mg2+‐ferrocytochrome system was measured. The thermodynamic parameters were found to be: ΔH0obs=+ 12 kcal/mol, ΔG0obs, (25°C) =−5.6 kcal/mol and ΔS0obs=+ 57 cal × mob1× K−1.
AB - The specific binding of cations to horse heart ferrocytochrome c has been studied, using the gel filtration method. The cations investigated were: Mg2+, Co2+, cinchonine and proflavine. The stability constants are in the range of 5–8 mM−1, and the number of binding sites per protein molecule are 1 to 2. The temperature dependence of the stability constant for the Mg2+‐ferrocytochrome system was measured. The thermodynamic parameters were found to be: ΔH0obs=+ 12 kcal/mol, ΔG0obs, (25°C) =−5.6 kcal/mol and ΔS0obs=+ 57 cal × mob1× K−1.
UR - http://www.scopus.com/inward/record.url?scp=0016211337&partnerID=8YFLogxK
U2 - 10.1111/j.1432-1033.1974.tb03631.x
DO - 10.1111/j.1432-1033.1974.tb03631.x
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C2 - 4368559
AN - SCOPUS:0016211337
SN - 0014-2956
VL - 46
SP - 387
EP - 391
JO - European Journal of Biochemistry
JF - European Journal of Biochemistry
IS - 2
ER -