Characterization of the glycine-dependent redox-cycling activity in animal fluids and tissues using specific inhibitors and activators: evidence for presence of PQQ.
Pyrroloquinoline quinone, a redox cofactor first isolated from bacteria, efficiently catalyzes the nonenzymatic oxidation of glycine in the presence of nitroblue tetrazolium. We report that certain metallic cations and heterocyclic aromatic cations, like the N-methyl phenazonium cation and aryl-iodonium compounds, strongly and specifically inhibit this redoxcycling activity. The inhibition by metal cations is reversed by Tiron and that of the aromatic cations by Tiron and thyroxine. These inhibitors and activators affect authentic PQQ and the redox-activity of putative PQQ isolated from biological sources in a similar manner. This indicates that pyrroloquinoline quinone occurs naturally in animal tissues and fluids.
Flückiger
R
R
Laboratory of Human Biochemistry, Children's Hospital, Boston, MA.
Paz
M
M
Mah
J
J
Bishop
A
A
Gallop
P M
PM
D000818:Animals; D001826:Body Fluids / Q000378:metabolism; D002412:Cations / Q000494:pharmacology; D005998:Glycine / Q000378:metabolism*; D008670:Metals / Q000494:pharmacology; D008892:Milk / Q000378:metabolism; D010084:Oxidation-Reduction / Q000187:drug effects; D045542:PQQ Cofactor; D015363:Quinolones / Q000302:isolation & purification / Q000378:metabolism*; D013347:Subcellular Fractions / Q000378:metabolism
D002412:Cations; D008670:Metals; D015363:Quinolones; D045542:PQQ Cofactor; D005998:Glycine