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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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Current Opinion in Structural Biology, 1996
Within the past year, the structures of the cytochrome c oxidase from the soil bacterium Paracoccus denitrificans and of the metal centers of the cytochrome c oxidase from bovine heart mitochondria, both determined at 2.8 A resolution by X-ray crystallography, have been reported. The structures form a basis for understanding the mechanism of this redox-
C, Ostermeier, S, Iwata, H, Michel
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Within the past year, the structures of the cytochrome c oxidase from the soil bacterium Paracoccus denitrificans and of the metal centers of the cytochrome c oxidase from bovine heart mitochondria, both determined at 2.8 A resolution by X-ray crystallography, have been reported. The structures form a basis for understanding the mechanism of this redox-
C, Ostermeier, S, Iwata, H, Michel
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International Journal of Biochemistry, 1978
Abstract Enzymatic methylation of 72 lysyl residue of cytochrome c in lower organisms facilitates its binding to mitochondria, and subsequently plays an important role in the electron transport ...
E, Polastro +4 more
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Abstract Enzymatic methylation of 72 lysyl residue of cytochrome c in lower organisms facilitates its binding to mitochondria, and subsequently plays an important role in the electron transport ...
E, Polastro +4 more
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Respiratory Cytochrome Supercomplexes
2016Evidence from several investigations demonstrates the existence of supramolecular units of Complex I, Complex III, and multiple copies of Complex IV in mitochondria and indicates that specific respiratory complexes may preferentially associate to form cytochrome-containing supercomplexes in the native membrane.
LENAZ, GIORGIO, GENOVA, MARIA LUISA
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