Differential Hydrogen Bonding in Human CYP17 Dictates Hydroxylation versus Lyase Chemistry1. Issue 20 (10th April 2013)

• Record Type: Journal Article
• Authors: Gregory, Michael; Mak, Piotr J.; Sligar, Stephen G.; Kincaid, James R.
• Is Part Of: Angewandte Chemie international edition. Volume 52:Issue 20(2013)
• Page Start: 5342
• Page End: 5345
• Publication Date: 2013-04-10
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201300760
• Languages: English
• ISSNs: 1433-7851

Abstract

<abstract abstract-type="graphical" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <bold>Consequences of alternative H‐bonding</bold>: Raman spectra of oxygenated intermediates of Nanodisc‐incorporated human CYP17 in the presence of natural substrates (pregnenolone and progesterone) directly confirm that substrate structure effectively alters hydrogen‐bonding interactions with the critical Fe–O–O fragment and dictates its predisposition for one of two alternative reaction pathways. Such substrate control has profound physiological implications.<boxed-text content-type="graphic" position="anchor" orientation="portrait"><graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgg1zsxhgvv" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></boxed-text></p> </abstract>