Linoleic acid positioning in psi factor producing oxygenase A, a fusion protein with an atypical cytochrome P450 activity
Article first published online: 7 OCT 2011
© 2011 The Authors Journal compilation © 2011 FEBS
Special Issue: Cytochrome P450 Structure and Function
Volume 279, Issue 9, pages 1594–1606, May 2012
How to Cite
Koch, C., Fielding, A. J., Brodhun, F., Bennati, M. and Feussner, I. (2012), Linoleic acid positioning in psi factor producing oxygenase A, a fusion protein with an atypical cytochrome P450 activity. FEBS Journal, 279: 1594–1606. doi: 10.1111/j.1742-4658.2011.08352.x
- Issue published online: 19 APR 2012
- Article first published online: 7 OCT 2011
- Accepted manuscript online: 15 SEP 2011 01:00PM EST
- (Received 24 June 2011, revised 2 September 2011, accepted 13 September 2011)
Fig. S1. Absorbance and CD spectra of PpoA_wt and various mutants.
Fig. S2. SDS/PAGE of purified PpoA wild type and variants.
Fig. S3. Identification of the peak eluting at 16.7 min as methyl ester of 5,8-DiHODE.
Fig. S4. 9-GHz EPR spectra of PpoA (75 μm) and N887V (75 μm).
Fig. S5. (A) 9-GHz CW spectrum at 70 K of the radical formed after reaction of either PpoA (75 μm) (black) or Y327F (blue) with 160-fold excess (8R)-HPODE. (B) 95-GHz Echo-detected spectrum (1-st derivative) of the radical formed after reaction of either PpoA (75 mm) (black) or Y327F (blue) with 160-fold excess (8R)-HPODE.
Fig. S6. Superimposition of the modeled DOX domain of PpoA and oPGHS-1.
Fig. S7. Superimposition of the structures of Arabidopsis thalania and Parthenium argentatum AOS.
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