Issue 21, 2004
From the journal:

Chemical Communications

Substrate binding and the presence of ferredoxin affect the redox properties of the soluble plant Δ9-18∶0-acyl carrier protein desaturase

V. Reipa,a   J. Shanklinb  and  V. Vilkera  

a Biotechnology Division, National Institute of Standards and Technology, Gaithersburg, USA
E-mail: vytas@nist.gov
Fax: 301 975 5449
Tel: 301 975 5056

b Department of Biology, Brookhaven National Laboratory, Upton, New York, USA
E-mail: shanklin@bnl.gov
Fax: 631 344 4407
Tel: 631 344 3414

Abstract

Substrate-free Δ9-18∶0-acyl carrier protein desaturase (abbreviated to Des) [E.C. # 1.14.99.6] was 2-electron reduced with E’0 = −0.03 + −0.01 V; the presence of spinach ferredoxin (SpFd) induces an additional 1-electron reduction wave at E’0 = −0.21 + −0.02 V, which shifts by 0.106 V upon substrate binding.

Graphical abstract: Substrate binding and the presence of ferredoxin affect the redox properties of the soluble plant Δ9-18∶0-acyl carrier protein desaturase

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Article information

DOI
https://doi.org/10.1039/B409595B
Article type
Communication
Submitted
23 Jun 2004
Accepted
17 Aug 2004
First published
23 Sep 2004

Chem. Commun., 2004, 2406-2407

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Substrate binding and the presence of ferredoxin affect the redox properties of the soluble plant Δ9-18∶0-acyl carrier protein desaturase

V. Reipa, J. Shanklin and V. Vilker, Chem. Commun., 2004, 2406 DOI: 10.1039/B409595B

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