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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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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.
P M, Epstein +4 more
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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 ...
P D, Barker +3 more
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Photoredox reactions in cytochrome c and cytochrome c551
Inorganica Chimica Acta, 1986Abstract A previously obtained photomodified cytochrome c is analyzed in order to characterize the first coordination sphere of the heme iron. Electron spin resonance and electrochemical measurements show that iron is exa-coordinated in the photomodified cytochrome as well as in the native one and are in favour of tyrosine-67 being the sixth heme ...
MALDOTTI, Andrea +5 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 ...
M J, Billen, E J, Squires
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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 ...
M J, Billen, E J, Squires
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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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Cytochrome P450s and chemoprevention
Biochemical Society Transactions, 2000The cytochrome P450 mono-oxygenase system represents a major defence against chemical challenge from the environment, constituting part of an adaptive response mounted by an organism following exposure to harmful agents. Cytochrome P450s are also able to catalyse the activation of compounds to toxic products, and participate in a variety of essential ...
Henderson, C J, Sahraouei, A, Wolf, C R
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