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Aizenman, E., Hartnett, K., Zhong, C., Gallop, P. and Rosenberg, P. (1992) Interaction of the putative essential nutrient pyrroloquinoline quinone with the n-methyl-d-aspartate receptor redox modulatory site. The Journal of Neuroscience, 12, 2362-2369.

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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.