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, 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.
Tabata
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Research Center for Biological Function, The Kitasato Institute and Graduate School of Pharmaceutical Sciences, Kitasato University, Tokyo, Japan.
Tomoda
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Omura
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D002352:Carrier Proteins / Q000037:antagonists & inhibitors*; D053480:Cholesterol Ester Transfer Proteins; D005296:Ferrous Compounds / Q000737:chemistry*; D006023:Glycoproteins; D009682:Magnetic Resonance Spectroscopy; D009603:Nitroso Compounds / Q000737:chemistry*; D013302:Streptomyces / Q000378:metabolism*
D002352:Carrier Proteins; D053480:Cholesterol Ester Transfer Proteins; D005296:Ferrous Compounds; D006023:Glycoproteins; D009603:Nitroso Compounds; C405055:ferroverdin B; C405056:ferroverdin C