A Periplasmic Binding Protein for Pyrroloquinoline Quinone

Research output: Contribution to journalArticle

Abstract

Pyrroloquinoline quinone (PQQ) is an essential redox cofactor in bacterial calcium- and lanthanide-dependent alcohol dehydrogenases. Although certain bacteria are known to synthesize and secrete PQQ, little is known about trafficking of this cofactor within and between cells. Here, we show that a previously uncharacterized periplasmic (solute) binding protein from Methylobacterium extorquens AM1, here renamed PqqT, binds 1 equiv of PQQ with high affinity (Kd = 50 nM). UV-visible and spectrofluorometric titrations establish that PqqT binds an unhydrated form of PQQ with distinct spectral features from the cofactor in free solution. To our knowledge, PqqT is the first solute-binding protein identified for PQQ and the first protein implicated in cellular trafficking of the cofactor. We propose that PqqT, which is encoded adjacent to a putative ATP-binding cassette transporter in the M. extorquens genome, is involved in uptake of exogenous PQQ to supplement endogenous cofactor biosynthesis. These results support the emerging importance of PQQ transfer within microbial and microbe-host communities.

Original languageEnglish (US)
Pages (from-to)2665-2669
Number of pages5
JournalBiochemistry
Volume58
Issue number23
DOIs
StatePublished - Jun 11 2019

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PQQ Cofactor
Periplasmic Binding Proteins
Methylobacterium extorquens
Carrier Proteins
Lanthanoid Series Elements
ATP-Binding Cassette Transporters
Alcohol Dehydrogenase
Biosynthesis
Titration
Oxidation-Reduction
Bacteria
Genes
Genome
Calcium

All Science Journal Classification (ASJC) codes

  • Biochemistry

Cite this

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abstract = "Pyrroloquinoline quinone (PQQ) is an essential redox cofactor in bacterial calcium- and lanthanide-dependent alcohol dehydrogenases. Although certain bacteria are known to synthesize and secrete PQQ, little is known about trafficking of this cofactor within and between cells. Here, we show that a previously uncharacterized periplasmic (solute) binding protein from Methylobacterium extorquens AM1, here renamed PqqT, binds 1 equiv of PQQ with high affinity (Kd = 50 nM). UV-visible and spectrofluorometric titrations establish that PqqT binds an unhydrated form of PQQ with distinct spectral features from the cofactor in free solution. To our knowledge, PqqT is the first solute-binding protein identified for PQQ and the first protein implicated in cellular trafficking of the cofactor. We propose that PqqT, which is encoded adjacent to a putative ATP-binding cassette transporter in the M. extorquens genome, is involved in uptake of exogenous PQQ to supplement endogenous cofactor biosynthesis. These results support the emerging importance of PQQ transfer within microbial and microbe-host communities.",
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A Periplasmic Binding Protein for Pyrroloquinoline Quinone. / Ho, Jackson V.; Cotruvo, Jr., Joseph Alfred.

In: Biochemistry, Vol. 58, No. 23, 11.06.2019, p. 2665-2669.

Research output: Contribution to journalArticle

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