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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M. R. Lemberg, “Cytochrome Oxidase” Gilmour, Lemberg, and Chance or Lemberg and Chance, unpublished observations, should now be: Gilmour, M. V., M. R. Lemberg, and B. Chance.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M. R. Lemberg, “Cytochrome Oxidase” Gilmour, Lemberg, and Chance or Lemberg and Chance, unpublished observations, should now be: Gilmour, M. V., M. R. Lemberg, and B. Chance.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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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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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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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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Phytochemistry, 1994
The present status of plant cytochrome P450 research is reviewed. A comparison of the properties of this group of cytochrome proteins with those of other microsomal b-type haem proteins is made. The range of reactions catalysed by P450s is discussed as well as recent progress in improving purification and reconstitution.
G P, Bolwell, K, Bozak, A, Zimmerlin
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The present status of plant cytochrome P450 research is reviewed. A comparison of the properties of this group of cytochrome proteins with those of other microsomal b-type haem proteins is made. The range of reactions catalysed by P450s is discussed as well as recent progress in improving purification and reconstitution.
G P, Bolwell, K, Bozak, A, Zimmerlin
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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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