Journal
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
Volume 1858, Issue 2, Pages 95-102Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbabio.2016.11.008
Keywords
Bacterial denitrification; Nitrous oxide reductase; Flavin binding protein; ApbE/NosX family protein; X-ray crystallography
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Funding
- European Research Council (ERC grant) [310656]
- European Research Council (ERC) [310656] Funding Source: European Research Council (ERC)
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The copper-containing enzyme nitrous oxide reductase (N2OR) catalyzes the transformation of nitrous oxide (N2O) to dinitrogen (N-2) in microbial denitrification. Several accessory factors are essential for assembling the two copper sites Cu-A and Cu-z, and for maintaining the activity. In particular, the deletion of either the transmembrane iron-sulfur flavoprotein NosR or the periplasmic protein NosX, a member of the ApbE family, abolishes N2O respiration. Here we demonstrate through biochemical and structural studies that the ApbE protein from Pseudomonas stutzeri, where the nosX gene is absent, is a monomeric FAD-binding protein that can serve as the flavin donor for NosR maturation via covalent flavinylation of a threonine residue. The flavin transfer reaction proceeds both in vivo and in vitro to generate post-translationally modified NosR with covalently bound FMN. Only FAD can act as substrate and the reaction requires a divalent cation, preferably Mg2+ that was also present in the crystal structure. In addition, the reaction is species-specific to a certain extent. (C) 2016 Elsevier B.V. All rights reserved.
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