Results 261 to 270 of about 754,856 (314)
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On cytochrome c oxidase II. The ratio of cytochrome a to cytochrome a3
Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation, 1966Summary 1. Cytochrome c oxidase was titrated, under anaerobic conditions, with NADH and phenazine methosulphate in the presence of chelating agents. Three different effects of chelating agents on the titration were found from which it can be concluded that cyanide and azide prevent the reduction of half the haem a and half the copper, EDTA and ...
B F, van Gelder, A O, Muijsers
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Cytochrome a and Cytochrome Oxidase
Nature, 1938A HEART muscle preparation obtained by a method previously described1 contains several dehydrogenases, a very powerful cytochrome oxidase and the three components (a, b, and c) of cytochrome. This material contains a high concentration of cytochrome a and is therefore very suitable for the study of this component.
D. KEILIN, E. F. HARTREE
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Fluorescence studies of cytochrome c1 and a cytochrome c1-cytochrome c complex
Biochemical and Biophysical Research Communications, 1974Summary Cytochrome c 1 and cytochrome c form a complex in aqueous solution. The complex is stable to chromatography on Sephadex but is dissociated in media of high ionic strength. Results from the fluorescence probe technique using 8-anilino-1-naphthaline sulphonic acid strongly suggest that (i) the heme group of cytochrome c 1 is completely ...
L S, Kaminsky +3 more
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Nature, 1958
A CYTOCHROME system appears to be involved in the oxidation of nitrite by Nitrobacter since, at normal temperatures, three cytochrome bands may be seen in suspensions of the cells in the presence of nitrite, but not in its absence. These are two sharp bands at 521 mµ and at 550 mµ and a more diffuse, less-intense band at about 589 mµ 1.
W D, BUTT, H, LEES
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A CYTOCHROME system appears to be involved in the oxidation of nitrite by Nitrobacter since, at normal temperatures, three cytochrome bands may be seen in suspensions of the cells in the presence of nitrite, but not in its absence. These are two sharp bands at 521 mµ and at 550 mµ and a more diffuse, less-intense band at about 589 mµ 1.
W D, BUTT, H, LEES
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Nature, 1958
IT has been concluded from experiments with barley leaves that chloroplasts contain cytochromes ƒ and b 6 and no cytochrome c 1. We have been able to extend the observations to two other widely differing species and to record certain characteristics of the cytochromes present.
W O, JAMES, R M, LEECH
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IT has been concluded from experiments with barley leaves that chloroplasts contain cytochromes ƒ and b 6 and no cytochrome c 1. We have been able to extend the observations to two other widely differing species and to record certain characteristics of the cytochromes present.
W O, JAMES, R M, LEECH
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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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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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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 W, König, J, Wilms, B F, Van Gelder
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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.
J, Stonehuerner +2 more
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Current Opinion in Structural Biology, 1995
Since 1993, three new cytochrome P450 X-ray structures have been determined, giving a total of four known structures. Two of the new structures are in the substrate-free form and one is substrate-bound. These new structures, together with a wealth of mutagenesis studies on various P450s, have provided considerable information on what structural ...
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Since 1993, three new cytochrome P450 X-ray structures have been determined, giving a total of four known structures. Two of the new structures are in the substrate-free form and one is substrate-bound. These new structures, together with a wealth of mutagenesis studies on various P450s, have provided considerable information on what structural ...
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