1992
DOI: 10.1016/0003-9861(92)90428-y
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Comparative study of monomeric reconstituted and membrane microsomal monooxygenase systems of the rabbit liver

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Cited by 26 publications
(16 citation statements)
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“…Thus, ligand binding on the distal side of the protein may partially mediate interaction with electron transfer partners on the proximal side. This is consistent with data showing that substrate binding both enhances reductase binding (35) and 2B4 reduction (36) over that of the substrate-free enzyme. The flexibility of helix I is also thought to be important in allowing diverse substrates to bind as well as in influencing redox partner binding (37) in at least some P450s.…”
Section: Discussionsupporting
confidence: 92%
“…Thus, ligand binding on the distal side of the protein may partially mediate interaction with electron transfer partners on the proximal side. This is consistent with data showing that substrate binding both enhances reductase binding (35) and 2B4 reduction (36) over that of the substrate-free enzyme. The flexibility of helix I is also thought to be important in allowing diverse substrates to bind as well as in influencing redox partner binding (37) in at least some P450s.…”
Section: Discussionsupporting
confidence: 92%
“…Mostly formation of oligomers has been inferred as an important aspect of structural organization in the native membrane bound state of the eukaryotic P450 enzymes [55-56, 60]. Possible functional implications of cytochromes P450 oligomerization in the membrane have been described in experimental reconstituted liposomal bilayers [56, 60, 101, 146-148], in detergent solubilized systems [55, 146, 149] and in the native membranes [55-56, 61]. Formation of oligomers can be an important source of cooperative effects in P450 systems, because of possible limited access of substrates to some monomers, different modes of interactions with reductases, and potential redistribution of the high affinity binding sites among the catalytically active and inactive ones.…”
Section: Cooperativity In Oligomers Of Cytochromes P450mentioning
confidence: 99%
“…Many investigations have shown that there are considerable differences present between these two cytochrome P450s concerning hydrophobicity and physicochemical properties. Cytochrome P450IIB4 is stable and highly soluble in detergent solution, and therefore this cytochrome has been extensively examined in terms of interactions with redox partners, membrane topology, and drug oxidation activity not only in detergent solutions but also in phospholipid vesicles (Davydov et al, 1992;Nishimoto et al, 1983;Sevrukova et al, 1994;Voznesensky & Schenkman, 1992, 1994. Cytochrome P450IA2 is very hydrophobic and was not, so far, successfully incorporated in phospholipid vesicles until the present work.…”
mentioning
confidence: 99%