Results 311 to 320 of about 778,750 (338)
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Interaction between cytochrome c and cytochrome b5
Biochemistry, 1979The reduction of cytochrome c by cytochrome b5 was studied over a wide range of ionic strengths in four different buffer systems. The reaction rate decreased linearly as the I1/2 was increased, suggesting that electrostatic interactions are important in the interaction.
Francis Millett +2 more
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Physiological Reviews, 1969
M. R. Lemberg, “Cytochrome Oxidase” Gilmour, Lemberg, and Chance or Lemberg and Chance, unpublished observations, should now be: Gilmour, M. V., M. R. Lemberg, and B. Chance. Cytochrome oxidase and its derivatives. 9. Spectrophotometric studies on the rapid reaction of ferrous cytochrome c oxidase with molecular oxygen under conditions of complete ...
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M. R. Lemberg, “Cytochrome Oxidase” Gilmour, Lemberg, and Chance or Lemberg and Chance, unpublished observations, should now be: Gilmour, M. V., M. R. Lemberg, and B. Chance. Cytochrome oxidase and its derivatives. 9. Spectrophotometric studies on the rapid reaction of ferrous cytochrome c oxidase with molecular oxygen under conditions of complete ...
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Conversion of Cytochrome b562 to c-Type Cytochromes
Biochemistry, 1995Cytochrome b562 from the periplasm of Escherichia coli is the only member of a family of cytochromes sharing the 4-alpha-helical bundle structural motif that does not have a covalently bound heme. We have introduced cysteine residues into the amino acid sequence of cytochrome b562 in positions homologous to those found in the other members of the ...
Edmund P. Nerou +3 more
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On cytochrome c oxidase I. The extinction coefficients of cytochrome a and cytochrome a3
Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation, 1966Summary 1. In agreement with Gibson, a shoulder at 420–424 m μ is present in the absorption spectra of preparations of cytochrome c oxidase (ferrocytochromec: oxygen oxidoreductase, EC 1.9.3.1) reduced with Na 2 S 2 O 4 . An examination of the spectra in the presence and absence of cyanide showed that this is due to the presence of equal amounts
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The reaction between cytochrome C1 and cytochrome C
Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1981The kinetics of electron transfer between the isolated enzymes of cytochrome c1 and cytochrome c have been investigated using the stopped-flow technique. The reaction between ferrocytochrome c1 and ferricytochrome c is fast; the second-order rate constant (k1) is 3.0 . 10(7) M-1 . s-1 at low ionic strength (I = 223 mM, 10 degrees C).
B.F. Van Gelder, J. Wilms, B.W. König
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Phosphorylation of cytochrome P450: Regulation by cytochrome b5
Archives of Biochemistry and Biophysics, 1989Rabbit liver cytochrome P450 LM2 and several forms of rat liver cytochrome P450 are phosphorylated by cAMP-dependent protein kinase (PKA) and by protein kinase C. Under aqueous assay conditions at neutral pH LM2 is phosphorylated only to a maximum extent of about 20 mol% by PKA.
Chi-Kuang Huang +4 more
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The Journal of Steroid Biochemistry and Molecular Biology, 2009
Male pigs are routinely castrated to prevent the accumulation of testicular 16-androstene steroids, in particular 5alpha-androst-16-en-3-one (5alpha-androstenone), which contribute to an off-odour and off-flavour known as boar taint. Cytochrome P450C17 (CYP17A1) catalyses the key regulatory step in the formation of the 16-androstene steroids from ...
E. J. Squires, M.J. Billen
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Male pigs are routinely castrated to prevent the accumulation of testicular 16-androstene steroids, in particular 5alpha-androst-16-en-3-one (5alpha-androstenone), which contribute to an off-odour and off-flavour known as boar taint. Cytochrome P450C17 (CYP17A1) catalyses the key regulatory step in the formation of the 16-androstene steroids from ...
E. J. Squires, M.J. Billen
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The oxidation of cytochrome c by cytochrome c peroxidase
Archives of Biochemistry and Biophysics, 1960Abstract 1. 1. The reaction between cytochrome c and cytochrome c peroxidase is first order in cytochrome c. 2. 2. The reaction is inhibited by both oxidized and reduced cytochrome c. 3. 3. The dependence of the reaction rate on ionic strength suggests that the reaction occurs at oppositely charged active sites on the two proteins. 4.
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2002
Cytochrome oxidase is the terminal oxidase of most of aerobic organisms and reduces molecular oxygen (O2) to water (1). The electrons and protons required for the formation of water molecules are transferred from both sides of the mitochondrial inner membranes in eukaryotic cells and of the cell membrane in prokaryotic cells (1).
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Cytochrome oxidase is the terminal oxidase of most of aerobic organisms and reduces molecular oxygen (O2) to water (1). The electrons and protons required for the formation of water molecules are transferred from both sides of the mitochondrial inner membranes in eukaryotic cells and of the cell membrane in prokaryotic cells (1).
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Photoredox reactions in cytochrome c and cytochrome c551
Inorganica Chimica Acta, 1986AbstractA previously obtained photomodified cytochrome c is analyzed by ESR and electrochemical measurements which show that iron is hexa‐coordinate in the photomodified cytochrome as well as in the native protein.
MALDOTTI, Andrea +5 more
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