1989
DOI: 10.1016/0167-4838(89)90091-5
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Cross-linking studies of the cholesterol hydroxylation system from bovine adrenocortical mitochondria

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Cited by 17 publications
(4 citation statements)
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“…However, before proceeding to a discussion of the new results obtained for the dioxygen adducts, to help clarify certain nebulous or incomplete results reported in previous studies, we undertook additional rR studies to further define active site structural differences that exist for the ferric and ferrous CO-bound forms with each of the three physiologically relevant substrates. In addition, these studies provide further definition of the effects of adrenodoxin binding on the heme structure and its interactions with active site structural elements, including the Fe–S bond between the heme and the cysteine residue, a functionally crucial linkage that can be manipulated by slight structural alterations within the proximal heme pocket where adrenodoxin binding occurs. …”
Section: Resultsmentioning
confidence: 99%
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“…However, before proceeding to a discussion of the new results obtained for the dioxygen adducts, to help clarify certain nebulous or incomplete results reported in previous studies, we undertook additional rR studies to further define active site structural differences that exist for the ferric and ferrous CO-bound forms with each of the three physiologically relevant substrates. In addition, these studies provide further definition of the effects of adrenodoxin binding on the heme structure and its interactions with active site structural elements, including the Fe–S bond between the heme and the cysteine residue, a functionally crucial linkage that can be manipulated by slight structural alterations within the proximal heme pocket where adrenodoxin binding occurs. …”
Section: Resultsmentioning
confidence: 99%
“…Interaction with natural or alternative reductases can alter the function and possibly the active site structure of the cytochrome P450. 1,2,14,23–25 Adrenodoxin (Adx), which contains a [2Fe-2S] cluster, is generally believed to serve as an electron shuttle between a NADPH containing enzyme, adrenodoxin reductase (AdR), and the active site of CYP11A1. 9,23–25 It has been reported that the inherent reduction potential of substrate-bound CYP11A1 is −284 mV, while that for Adx is −273 mV, with protein-protein complex formation causing the reduction potential of Adx to undergo a small negative shift to −291 mV, while that of the CYP11A1 shifts to −312 mV.…”
Section: Introductionmentioning
confidence: 99%
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“…lion of' cyt~hrome b; and =drenodoxln for bindinil with cytochrom¢ P-450scc suilaests that a similar cationic site on the surface of cytochrome P.4~0scc is involved in the alas©clarion with both prot=ins. Indeed, recently we halve shown by chemical modification and cross.linking experiments that positively charged residues of the N-and C.terminal sequence of cytochrome P.450scc are involved in the electrostatic interaction with adrenodoxin [8,9], The similancy of the processes of the interaction of cytochrome P.4505cc with cytochrom¢ b= and adrenodoxin allowed us to propose that adrenodoxin m~$ht interact with cyLochrome P.450 from endopiasmic reticulum membranes. Indeed, the mteraclion of adrenodoxin with some microsomal cytochrome P-450 isozymes has been demonstrated using spectral titration, affinity, chromatography and reconst~tution experiments (unpublished results).…”
Section: Discussionmentioning
confidence: 99%