1979
DOI: 10.1016/0006-291x(79)91916-8
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Spin state control of the hepatic cytochrome P450 redox potential

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Cited by 124 publications
(95 citation statements)
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“…With rat CPR, they are E m (FAD semiquinone/reduced ) = −0.365 V, E m (FAD oxidized/semiquinone ) = −0.290 V, E m (FMN semiquinone/reduced ) = −0.270 V and E m (FMN oxidized/semiquinone ) = −0.110 V vs NHE [23] (see also Table 1). On the other hand, the midpoint potentials of substrate (hexobarbital)-bound rat liver cytochrome P450 and microsomal cytochrome b 5 have been reported to be −0.237 V [37] and 0.02 V vs NHE [38], respectively. In the present study, the midpoint potential of the ferric/ferrous couple in the heme-rHO-1 complex was found to be −0.087 V vs NHE.…”
Section: Discussionmentioning
confidence: 99%
“…With rat CPR, they are E m (FAD semiquinone/reduced ) = −0.365 V, E m (FAD oxidized/semiquinone ) = −0.290 V, E m (FMN semiquinone/reduced ) = −0.270 V and E m (FMN oxidized/semiquinone ) = −0.110 V vs NHE [23] (see also Table 1). On the other hand, the midpoint potentials of substrate (hexobarbital)-bound rat liver cytochrome P450 and microsomal cytochrome b 5 have been reported to be −0.237 V [37] and 0.02 V vs NHE [38], respectively. In the present study, the midpoint potential of the ferric/ferrous couple in the heme-rHO-1 complex was found to be −0.087 V vs NHE.…”
Section: Discussionmentioning
confidence: 99%
“…Microsomal cytochrome b 5 (cyt b 5 ) 1 is an amphipathic electron transfer hemoprotein located in the membrane of the endoplasmic reticulum. It provides electrons for a broad range of reactions, including fatty acid desaturation, cholesterol biosynthesis, and a variety of cytochrome P450-dependent oxidation and hydroxylation reactions (1,2).…”
mentioning
confidence: 99%
“…Both ferric and oxyferrous cyt P450 receive electrons from NADPH via its redox partner, NADPH-cytochrome P450 reductase (cyt P450 reductase), whereas cyt b 5 can donate the second electron. Because of the high redox potential of Х20 mV for cyt b 5 , the first electron required to reduce cyt P450 from the ferric to the ferrous state is always transferred from NADPH via cyt P450 reductase. However, as the redox potential of cyt P450 increases from ХϪ230 mV to ϩ50 mV on transition to the oxyferrous state, the second electron can be obtained from either cyt P450 reductase or cyt b 5 (5,6).…”
mentioning
confidence: 99%
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