WrbA bridges bacterial flavodoxins and eukaryotic NAD(P)H: quinone oxidoreductases

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Bibtex

@article{c9fee7fb95f4475886be70bb263bf4ea,
title = "WrbA bridges bacterial flavodoxins and eukaryotic NAD(P)H: quinone oxidoreductases",
abstract = "The crystal structure of the flavodoxin-like protein WrbA with oxidized FMN bound reveals a close relationship to mammalian NAD(P) H:quinone oxidoreductase, Nqo1. Structural comparison of WrbA, flavodoxin, and Nqo1 indicates how the twisted open-sheet fold of flavodoxins is elaborated to form multimers that extend catalytic function from one-electron transfer between protein partners using FMN to two-electron reduction of xenobiotics using FAD. The structure suggests a novel physiological role for WrbA and Nqo1.",
keywords = "vitamin K, menaquinone, peripheral membrane proteins, soluble quinones, membrane quinones, chemotherapeutics, shikimate",
author = "Jannette Carey and Jiri Brynda and Julie Wolfova and Rita Grandori and Tobias Gustavsson and Ruediger Ettrich and Smatanova, {Ivana Kuta}",
year = "2007",
doi = "10.1110/ps.073018907",
language = "English",
volume = "16",
pages = "2301--2305",
journal = "Protein Science",
issn = "1469-896X",
publisher = "The Protein Society",
number = "10",

}