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Results for “PQQ Cofactor”

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PubMed1994

Biotin production by bifidobacteria.

Biotin production and the growth of the strains of Bifidobacterium adolescentis, B. bifidum, B. breve, B. infantis, and B. longum were studied. These five strains showed heavy growth on BL medium. But when yeast extract medium (carbon source, glucose) was used, the extent of their growth was significantly decreased, one-half or less than that of the growth on BL medium. B. bifidum grew well on yeast extract medium containing oligosaccharides, such as isomaltooligosaccharide, and produced biotin extracellularly. The utilization of oligosaccharides in biotin production by these five strains was investigated.

Bifidobacterium↗
PubMed1999

Characterization of the membrane quinoprotein glucose dehydrogenase from Escherichia coli and characterization of a site-directed mutant in which histidine-262 has been changed to tyrosine.

The requirements for substrate binding in the quinoprotein glucose dehydrogenase (GDH) in the membranes of Escherichia coli are described, together with the changes in activity in a site-directed mutant in which His262 has been altered to a tyrosine residue (H262Y-GDH). The differences in catalytic efficiency between substrates are mainly related to differences in their affinity for the enzyme. Remarkably, it appears that, if a hexose is able to bind in the active site, then it is also oxidized, whereas some pentoses are able to bind (and act as competitive inhibitors), but are not substrates. The activation energies for the oxidation of hexoses and pentoses are almost identical. In a previously published model of the enzyme, His262 is at the entrance to the active site and appears to be important in holding the prosthetic group pyrroloquinoline quinone (PQQ) in place, and it has been suggested that it might play a role in electron transfer from the reduced PQQ to the ubiquinone in the membrane. The H262Y-GDH has a greatly diminished catalytic efficiency for all substrates, which is mainly due to a marked decrease in their affinities for the enzyme, but the rate of electron transfer to oxygen is unaffected. During the processing of the PQQ into the apoenzyme to give active enzyme, its affinity is markedly dependent on the pH, four groups with pK values between pH7 and pH8 being involved. Identical results were obtained with H262Y-GDH, showing that His262 it is not directly involved in this process.

Amino Acid Substitution↗
PubMed1992

Pyrroloquinoline quinone (coenzyme PQQ) and the oxidation of SH residues in proteins.

Pyrroloquinoline quinone (PQQ) catalyzes the oxidation of cysteamine at neutral pH with a second order rate constant K2 = 0.45 M-1 s-1. The reduction of PQQ was monitored by absorption and fluorescence spectroscopy, whereas the oxidation of cysteamine to cystamine was followed by titration with 5,5'-dithiobis(2-nitrobenzoic acid). PQQ also catalyzes the oxidation of thiol groups critically connected with the function of two proteins, i.e. thioredoxin and phosphoribulose kinase. The reaction of PQQ with reduced thioredoxin brings about the oxidation of two thiol groups of the oxireductase, whereas the enzyme phosphoribulose kinase is inactivated at 25 degrees C. The oxidized disulfide bond of phosphoribulose kinase is reduced by dithiothreitol and the enzyme recovers catalytic activity. The ability of PQQ to catalyze the oxidation of vicinal cysteinyl residues to generate disulfide bonds under mild experimental conditions can be exploited to define the precise role of modified thiol residues in either catalysis or stabilization of protein structure.

Catalysis↗
PubMed1992

Interaction of the putative essential nutrient pyrroloquinoline quinone with the N-methyl-D-aspartate receptor redox modulatory site.

The putative essential nutrient pyrroloquinoline quinone (PQQ) can efficiently mediate reduction and oxidation reactions in a variety of systems. Therefore, we investigated whether this compound could alter the function of the NMDA receptor via a recently described redox modulatory site. In rat cortical neurons in vitro, 50 microM PQQ could reverse the enhancement of 30 microM NMDA-induced whole-cell ionic currents produced by the reducing agent dithiothreitol (DTT; 2-4 mM). PQQ also depressed native responses in a DTT-reversible fashion. In addition, 50-200 microM PQQ produced a significant degree of neuroprotection in an acute model of NMDA-mediated neurotoxicity in astrocyte-rich cultures of rat cerebral cortex. Under certain conditions, PQQ can lead to the formation of oxygen-derived free radicals, and we have previously observed that these reactive species can oxidize the NMDA receptor. Nevertheless, the enzymatic free radical scavengers superoxide dismutase and catalase (10 micrograms/ml each) did not abolish the actions of PQQ. This observation held true even in astrocyte-poor cortical cultures, where neuronal processes are directly exposed to the extracellular milieu. Therefore, under in vitro conditions in which PQQ is presented without an exogenous electron donor, it appears as if the entire neuroprotective effect of PQQ is attributable to a direct oxidation of the NMDA receptor redox site. These results suggest the possibility of a novel role for PQQ, PQQ-like substances, and quinone-containing proteins in the brain, and may represent a novel therapeutic approach for the amelioration of NMDA receptor-mediated neurotoxic injury.

Animals↗
PubMed1992

Wither PQQ.

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Amine Oxidase (Copper-Containing)↗
PubMed1992

The three-dimensional structures of methanol dehydrogenase from two methylotrophic bacteria at 2.6-A resolution.

The structures of methanol dehydrogenase (MEDH) from two closely related methylotrophic bacteria, Methylophilus methylotrophus and W3A1, have been determined at 2.6-A resolution. The molecule, a quinoprotein of molecular mass of about 138 kDa, contains two heavy (H) and two light (L) subunits of unknown sequence and two molecules of noncovalently associated pyrroloquinoline quinone. The two enzymes crystallize isomorphously in space group P2(1) with one H2L2 heterotetramer in the asymmetric unit. The electron density map of the M. methylophilus enzyme was obtained by multiple isomorphous replacement with anomalous scattering and improved by solvent leveling and electron density averaging. For model building, the amino acid sequence of MEDH from Paracoccus denitrificans for the H subunit and from Methylobacterium extorquens AM1 for the L subunit were used to represent the unknown amino acid sequence. At the present time, 579 and 57 amino acid residues for the large and small subunits, respectively, have been fitted into the map. The phases for MEDH from M. methylophilus were used directly to analyze the W3A1 structure, and both structures were refined to R-factors (where R = sigma[Fo-Fc[/sigma Fo) of 0.277 and 0.266, respectively. The L subunit contains a long alpha-helix and an extended N-terminal segment, both lying on the molecular surface of the H subunit. The H subunit contains eight antiparallel beta-sheets, each consisting of four strands arranged topologically like the letter W. The eight Ws are arranged circularly, forming the main disc-shaped body of the subunit, with some short helices and loops connecting the consecutive Ws, as well as some excursions within and between some of the Ws. The pyrroloquinoline quinone prosthetic group is located in the central channel of the large subunit near the surface of the molecule. The topology of the eight-W folding unit is similar to those of the six- and seven-W folding units previously reported for three other proteins, neuraminidase, methylamine dehydrogenase, and galactose oxidase.

Alcohol Oxidoreductases↗
PubMed1990

Quinoproteins: a new class of enzymes with potential use as biosensors.

The field of the enzymology of quinoproteins is still in its infancy. As more progress is made toward understanding the mechanisms of catalysis and electron transfer by protein-bound PQQ, it will become possible to more logically design specific quinoprotein-based electrodes. The characterization of new quinoproteins is progressing at a rapid rate. As new quinoproteins are found, the potential range of applications for use of these enzymes in biosensors will increase as well.

Bacteria↗
PubMed2005

Pyrroloquinoline quinone enhances regeneration of transected sciatic nerve in rats.

OBJECTIVE: To investigate the effect of pyrroloquinoline quinone (PQQ) on nerve regeneration of transected sciatic nerve in animal models. METHODS: Forty SD rats weighing 220-240 g were randomized into a PQQ group (n = 20) and a control group (n = 20). Each animal underwent sciatic nerve transection operation. After the operation, PQQ 0.5 ml (250 microg/Kg) was injected at the operation site in the PQQ group, while the same volume of normal saline was delivered in the control group. Nerve functional evaluation, electrophysiological index recording were carried out according to the experimental design. Newly generated nerve specimens were harvested 12 weeks postoperatively for morphological studies. RESULTS: In the PQQ group there was a good nerve regeneration and the sciatic nerve function, sciatic nerve function index, electrophysiological index and morphological appearance were superior to the control group (P < 0.05). CONCLUSIONS: PQQ has a remarkable effect in enhancing nerve regeneration of transected peripheral nerve.

Animals↗
PubMed1991

Direct evidence of the Entner-Doudoroff pathway operating in the metabolism of D-glucosamine in bacteria.

Pseudomonas fluorescens (Migula) (IFO 14808) has both a membrane-bound PQQ-dependent D-glucose (D-Glc) dehydrogenase [EC 1.1.99.17] [which also acts on D-glucosamine (D-GlcN)] and a PLP-dependent D-glucosaminate (D-GlcNA) dehydratase [EC 4.2.1.26]. Further, these two enzymes were induced when D-GlcN was added to the culture medium. However, D-glucosamine-6-phosphate (D-GlcN-6-P) isomerase [EC 5.3.1.10], another enzyme involved in the metabolism of D-GlcN, was only present at a low level in this bacterium. The bacterium was able to grow in a minimal medium containing D-GlcN or D-GlcNA as the sole source of carbon and nitrogen. Intact cells of P. fluorescens (Migula) converted D-GlcN to D-GlcNA and then to 2-keto-3-deoxy-D-gluconate (KDGA). These results demonstrate that D-GlcN is metabolized via D-GlcNA to KDGA in P. fluorescens (Migula) (Entner-Doudoroff pathway). In contrast, Enterobacter cloacae(IFO 13535) and Agrobacterium radiobacter (IAM 1526) have significant amounts of D-GlcN-6-P isomerase with low levels of the D-Glc dehydrogenase and D-GlcNA dehydratase. Further, only the isomerase activity was induced on the addition of D-GlcN to the culture medium. These results demonstrate that there is a new route (Entner-Doudoroff pathway), i.e., in addition to the known one (Embden-Meyerhof pathway), for the metabolism of D-GlcN in bacteria and one of the two routes is predominant in the each of bacteria examined.

Aldose-Ketose Isomerases↗
PubMed1990

New biological properties of pyrroloquinoline quinone and its related compounds: inhibition of chemiluminescence, lipid peroxidation and rat paw edema.

Pyrroloquinoline quinone (PQQ) inhibited the chemiluminescence (CL) from mouse peritoneal cells initiated by zymosan, carrageenin and N-formyl-methionyl-leucyl-phenylalanine and CL generated by the xanthine-xanthine oxidase reaction and the lipid peroxidation in the rat brain homogenate. The inhibitory activity of PQQ was more potent than that of idebenone, alpha-tocopherol and ascorbic acid in all the three assay systems. In the xanthine-xanthine oxidase reaction, PQQ had no effect on the formation of uric acid at the concentration of CL inhibition. These results suggest that PQQ might have a radical scavenger-like activity. Structure-activity relationship of PQQ and its six related compounds showed that the 7- and 9-carboxyl groups of PQQ as well as the orthoquinone structure are responsible for the radical scavenger-like activity. In addition, the -NH group in the pyrrole ring of PQQ seemed to be essential for the antilipid peroxidative activity in the rat brain homogenate. When administered i.p., PQQ inhibited the development of 0.1% carrageenin-induced paw edema in rats. These results suggest that PQQ might have therapeutic effects on various diseases, of which development or exacerbation has been known to be associated with radical oxygens.

Animals↗
PubMed1989

Nephrotoxicity of pyrroloquinoline quinone in rats.

When pyrroloquinoline quinone (PQQ) was intraperitoneally injected into rats daily for 4 days at a dose of 11.5 mg/kg body weight/injection, functional and morphologic changes of the kidneys were clearly observed. The most prominent finding was necrotic and degenerative changes of the proximal tubular epithelium as well as hematuria and an elevation of serum creatinine concentration.

Animals↗
PubMed1989

Spectral studies of bovine dopamine beta-hydroxylase. Absence of covalently bound pyrroloquinoline quinone.

Bovine dopamine beta-hydroxylase was examined spectroscopically for the presence of covalently bound pyrroloquinoline quinone (PQQ). Pure dopamine beta-hydroxylase had a featureless UV-visible spectrum above 300 nm. An equimolar solution of dopamine beta-hydroxylase and exogenously added PQQ (1 PQQ/active site) had a strong absorption maximum at 333 nm. Dialysis removed the added PQQ, indicating that dopamine beta-hydroxylase does not bind PQQ irreversibly. Reaction of dopamine beta-hydroxylase with 6 mM phenylhydrazine in the presence of 15 mM ascorbate caused 96% inactivation within 20 min and did not produce any spectrally detectable amounts of the phenylhydrazone adduct of PQQ, as reported by van der Meer et al. (van der Meer, R.A., Jongejan, J.A., and Duine, J.A. (1988) FEBS Lett. 231, 303-307). The peptide profile of phenylhydrazine inactivated dopamine beta-hydroxylase was monitored at 316 nm and did not reveal any peptides that might contain a PQQ-phenylhydrazone adduct. Thus, the absence of any spectrally detectable PQQ-phenylhydrazone adducts under these conditions demonstrates that the mechanism of phenylhydrazine inactivation does not involve covalent modification of PQQ at the active site of dopamine beta-hydroxylase and provides strong evidence that the native enzyme does not contain PQQ.

Adrenal Medulla↗