Abstract:
:The pre-steady-state reduction of cytochrome P450 (P450) 2B4 by P450 reductase (reductase) was modeled by assuming that an equilibrium between three catalytic conformers of P450 regulates the multi-phasic reduction of the enzyme. This model was compared to a model of reduction involving a minimum number of phases. Based on several criteria, the former model seems to provide an improved fit to the reduction data. Substrates were divided into two groups based on their effects at different concentrations of reductase. Surprisingly, in the presence of some substrates (group 1) but not others (group 2), the rate of reduction was actually slower with an excess of reductase than with equimolar reductase and P450. Presumably, oxidized reductase binds differently to P450 than reduced reductase. A schematic model based on two sites of interaction between reductase and P450 2B4 is offered to explain the unusual reduction kinetics with the two different groups of substrates.
journal_name
J Inorg Biochemjournal_title
Journal of inorganic biochemistryauthors
Reed JR,Hollenberg PFdoi
10.1016/s0162-0134(03)00310-6subject
Has Abstractpub_date
2003-11-01 00:00:00pages
276-86issue
3eissn
0162-0134issn
1873-3344pii
S0162013403003106journal_volume
97pub_type
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journal_title:Journal of inorganic biochemistry
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journal_title:Journal of inorganic biochemistry
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journal_title:Journal of inorganic biochemistry
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journal_title:Journal of inorganic biochemistry
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