Title : Anion-specific interaction with human NQO1 inhibits flavin binding.

Pub. Date : 2019 Apr 1

PMID : 30615965






3 Functional Relationships(s)
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1 In this work, binding of anions to the FAD binding pocket of human NAD(P)H:quinone oxidoreductase 1 (NQO1), a flavoprotein associated with cancer due to a common polymorphism causing a P187S amino acid substitution, was investigated. Flavin-Adenine Dinucleotide NAD(P)H quinone dehydrogenase 1 Homo sapiens
2 In this work, binding of anions to the FAD binding pocket of human NAD(P)H:quinone oxidoreductase 1 (NQO1), a flavoprotein associated with cancer due to a common polymorphism causing a P187S amino acid substitution, was investigated. Flavin-Adenine Dinucleotide NAD(P)H quinone dehydrogenase 1 Homo sapiens
3 Herein, binding and protein stability analyses were carried out to show that anion binding to the apo-state of NQO1 P187S inhibits FAD binding with increasing strength following the chaotropic behavior of anions. Flavin-Adenine Dinucleotide NAD(P)H quinone dehydrogenase 1 Homo sapiens