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- W1729971829 abstract "Publisher Summary This chapter presents a review of the structural and functional aspects of the flavoenzyme and ferredoxin type electron transfer proteins of the mitochondrial, microsomal, and bacterial P450 systems. The studies summarized in the chapter establish several general principles for P450 system electron transport chains: (1) The reductases are generally expressed at much lower levels than P450s, there being only one molecule of reductase per about 10 or more molecules of P450. (2) The protein components are independently mobile and do not form static multicomponent complexes. (3) Proteins that are redox partners form transient high affinity 1:1 complexes during their random diffusions, in accordance with the principles of mass action. Dissociation constants of these protein–protein complexes are strongly influenced by the redox states of the proteins and other molecules in the environment such as P450 substrate, ions, and phospholipids. (4) The transfer of an electron between two redox partners depends on the formation of a specific high affinity 1:1 complex between the two proteins. In P450 systems, electron transfer is not always coupled to substrate monooxygenation. P450s and their electron transfer proteins may transfer electrons to other acceptors, such as O 2 . This type of uncoupling or leaky electron transport is observed in both mitochondrial and microsomal systems." @default.
- W1729971829 created "2016-06-24" @default.
- W1729971829 creator A5091124254 @default.
- W1729971829 date "1996-01-01" @default.
- W1729971829 modified "2023-09-23" @default.
- W1729971829 title "Electron Transfer Proteins of Cytochrome P450 Systems" @default.
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