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Seedorf, H., et al. (2007) Structure of coenzyme F420H2 oxidase (FprA), a di-iron flavoprotein from methanogenic archaea catalyzing the reduction of O2 to H2O. FEBS Journal, 274, 1588-1599. doi:10.1111/j.1742-4658.2007.05706.x

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• TITLE: Crystal structure of PqqB from Pseudomonas putida at 2.2 Å resolution

  AUTHORS: Moritz Metlitzky, Sandra Puehringer, Stuart J. Fisher

  KEYWORDS: PqqB; PQQ; Biosynthetic Pathway; X-Ray Crystallography

  JOURNAL NAME: Journal of Biophysical Chemistry, Vol.3 No.2, May 29, 2012

  ABSTRACT: Pyrroloquinoline quinone (PQQ) is an important redox-active cofactor for many bacterial dehy-drogenases. It's biosynthetic pathway involves six or seven genes, one of which is pqqB. Former studies indicated that the protein encoded by pqqB, namely PqqB, functions as a PQQ transporter. Here we report the crystal structure of PqqB from Pseudomonas putida at 2.2 ? resolution together with functional studies to verify this theory.