title: Substrate binding and the presence of ferredoxin affect the redox properties of the soluble plant Delta9-18:0-acyl carrier protein desaturase.
abstract: Substrate-free Delta9-18:0-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.
authors.affiliation: Biotechnology Division, National Institute of Standards and Technology, Gaithersburg, MD 20899, USA. vytas@nist.gov
authors.forename: V
authors.initials: V
authors.lastname: Reipa
authors.forename: J
authors.initials: J
authors.lastname: Shanklin
authors.forename: V
authors.initials: V
authors.lastname: Vilker
mesh_terms: D004563:Electrochemistry; D004583:Electrons; D044943:Fatty Acid Desaturases / Q000737:chemistry*; D005288:Ferredoxins / Q000737:chemistry*; D006899:Mixed Function Oxygenases / Q000737:chemistry*; D010084:Oxidation-Reduction; D010940:Plant Proteins / Q000737:chemistry*; D012995:Solubility
chemical_list: D005288:Ferredoxins; D010940:Plant Proteins; D006899:Mixed Function Oxygenases; D044943:Fatty Acid Desaturases; C018747:acyl-(acyl-carrier-protein)desaturase