This work was supported by the National Institutes of Health grants GM31756 to S.G.S. and R01GM96117 to J.R.K.
Differential Hydrogen Bonding in Human CYP17 Dictates Hydroxylation versus Lyase Chemistry†
Article first published online: 10 APR 2013
Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Angewandte Chemie International Edition
Volume 52, Issue 20, pages 5342–5345, May 10, 2013
How to Cite
Gregory, M., Mak, P. J., Sligar, S. G. and Kincaid, J. R. (2013), Differential Hydrogen Bonding in Human CYP17 Dictates Hydroxylation versus Lyase Chemistry . Angew. Chem. Int. Ed., 52: 5342–5345. doi: 10.1002/anie.201300760
- Issue published online: 3 MAY 2013
- Article first published online: 10 APR 2013
- Manuscript Received: 28 JAN 2013
- National Institutes of Health. Grant Numbers: GM31756, R01GM96117
- heme proteins;
- Raman spectroscopy
Consequences of alternative H-bonding: 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.