The class
Ferroverdins B and C, natural CETP inhibitors from Streptomyces, are elucidated as iron complexes of nitroso-hydroxybenzoate ligands (J Antibiot (Tokyo) 1999)
Original title: Ferroverdins, inhibitors of cholesteryl ester transfer protein produced by Streptomyces sp. WK-5344. II. Structure elucidation
The structures of ferroverdins B and C, novel inhibitors of cholesteryl ester transfer protein produced by Streptomyces sp. WK-5344, were elucidated by spectroscopic studies including various NMR measurements. Both compounds are complexes of one Fe2+ ion with three ligands: ferroverdin B comprises two common p-vinylphenyl-3-nitroso-4-hydroxybenzoates and one hydroxy p-vinylphenyl-3-nitroso-4-hydroxybenzoate, while ferroverdin C comprises one carboxylic acid p-vinylphenyl-3-nitroso-4-hydroxybenzoate in place of the hydroxy ligand.
Original abstract
The structures of ferroverdins B and C, novel inhibitors of cholesteryl ester transfer protein, were elucidated by spectroscopic studies including various NMR measurements. They are the complex between one Fe2+ and three ligands, that is, two common p-vinylphenyl-3-nitroso-4-hydroxybenzoates and one hydroxy p-vinylphenyl-3-nitroso-4-hydroxybenzoate for ferroverdin B and one carboxylic acid p-vinylphenyl-3-nitroso-4-hydroxybenzoate for ferroverdin C.
Summary written by cetpinhibition.org from the published abstract; figures as published. Page updated 19 August 2026. Methods.