定制一种外来铁氧还蛋白以支持类似天然的 P450 单加氧酶活性。
Tailoring an alien ferredoxin to support native-like P450 monooxygenase activity.
机构信息
The School of Chemistry and Physics, The University of Adelaide, SA, Australia.
出版信息
Chem Commun (Camb). 2012 Dec 11;48(95):11692-4. doi: 10.1039/c2cc35968e.
PMID:23104016
Abstract
A ferredoxin associated with biological Fe-S cluster assembly has been remodelled to transfer electrons to a P450 enzyme and support substrate oxidation at 80% of the physiological ferredoxin activity, opening up the possibility of tailoring ferredoxins to reconstitute the activity of P450 enzymes for which the electron transfer partner proteins are not known.
摘要
一种与生物 Fe-S 簇组装相关的铁氧还蛋白已被改造，以将电子转移到 P450 酶，并支持底物氧化，其活性达到生理铁氧还蛋白活性的 80%，为定制铁氧还蛋白以恢复电子转移伙伴蛋白未知的 P450 酶的活性开辟了可能性。
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