Structure and stereochemistry of products of hydroxylation of human steroid hormones by a housefly cytochrome P450 (CYP6A1) | Zendy

Jacobsen Neil E. | Zendy; Kövér Katalin E. | Zendy; Murataliev Marat B. | Zendy; Feyereisen René | Zendy; Walker F. Ann | Zendy

Premium

Structure and stereochemistry of products of hydroxylation of human steroid hormones by a housefly cytochrome P450 (CYP6A1)

Author(s) -

Jacobsen Neil E.,

Kövér Katalin E.,

Murataliev Marat B.,

Feyereisen René,

Walker F. Ann

Publication year - 2006

Publication title -

magnetic resonance in chemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.483

H-Index - 72

eISSN - 1097-458X

pISSN - 0749-1581

DOI - 10.1002/mrc.1767

Subject(s) - chemistry , heteronuclear molecule , heteronuclear single quantum coherence spectroscopy , stereochemistry , two dimensional nuclear magnetic resonance spectroscopy , hydroxylation , cytochrome p450 , steroid , cytochrome b5 , nuclear magnetic resonance spectroscopy , enzyme , biochemistry , hormone

The structure and stereochemistry of nine steroid metabolites isolated in quantities ranging from 0.15 to 1.8 mg were determined using a variety of NMR techniques, including heteronuclear multiple bond correlation (HMBC) using broadband adiabatic 13 C pulses and phase‐sensitive data presentation. Testosterone, androstenedione and progesterone were oxidized with housefly cytochrome P450 6A1 enzyme reconstituted in vitro with housefly NADPH cytochrome P450 reductase and cytochrome b 5 . NMR analysis in CD 3 OD using a modified HMBC sequence as well as 2D heteronuclear single quantum correlation (HSQC), COSY and nuclear Overhauser and exchange spectroscopy (NOESY), combined with a detailed analysis of J couplings showed that hydroxylation occurs exclusively on the β‐face of the steroids, at positions 2, 12, and 15. Copyright © 2006 John Wiley & Sons, Ltd.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here

Accelerating Research