Pyrroloquinoline quinone (PQQ) which is popularly named as methoxatin, is a redox cofactor. It is ascertained in soil and fruits like kiwifruit, as well as human breast milk. Enzymes accommodating PQQ are called quinoproteins. Glucose dehydrogenase, the totality of the quinoproteins, is utilized essentially a glucose sensor. PQQ stimulates growth in bacteria.

Pyrroloquinoline quinone (PQQ) acts as a novel growth factor in both plants and animals. Pyrroloquinoline quinone acid powder (PQQ) influences energy-related metabolism and neurologic functions in animals.

However, little is known about the response to PQQ in humans. The reduced form of PQQ is a potent antioxidant and capable of catalyzing continuous and repeated oxidation and reduction reactions in chemical assays. For example, PQQ is 100–1000 times more efficient than other quinone bio factors in assays designed to assess redox cycling


Glutamic acid and tyrosine in PqqA are cross-linked by the radical SAM enzyme PqqE in the first step of PqqA modification. Struggles to concede PQQ biosynthesis have presented to broad concern in radical SAM enzymes and their capacity to transform proteins and a similar radical SAM enzyme-dependent pathway has considering been discovered that produces the putative electron transmitter mycofactocin, adopting a valine and a tyrosine from the precursor peptide, MFA.


The mechanism of action in animal models and cultured cells involves the activation or expression of factors, such as peroxisome proliferator-activated receptor alpha; cAMP response element-binding; nuclear respiratory factors 1 and 2; transcription factor A, mitochondrial; and peroxisome proliferator-activated receptor-γ coactivator 1-alpha.

Each of these transcription factors and coactivators plays a central role in the regulation of cellular energy metabolism (e.g., promotion of β-oxidation) and mitochondrial biogenesis and are related to the remodeling of muscle mass to a fiber-type combination that is metabolically added oxidative and concise glycolytic.

In addition, genes important to cellular stress (e.g., thioredoxin), cell signaling (Janus kinase-, MAPK- and STAT-related pathways) and nutrient transport are affected, which suggests that PQQ may act initially through cell surface cytokine and/or growth factor receptors or by influencing the phosphorylation of key components.


In summary, PQQ influences a wide range of systemic responses ranging from the stimulation of reproductive performance and neonatal growth in animal models fed highly refined diets to modulation in mitochondrial content and β-oxidation potential at dietary levels of exposure that are one to two orders of magnitudes below those required for bio factors, such as resveratrol.

Further, when the responses to PQQ are compared to other vitamins with redox cycling activity (e.g., ascorbic acid), the actions are often the opposite of those observed for PQQ, i.e., a reduction or no change in mitochondrial biogenesis or function.

The data included assistance like Resveratrol at  in the theory that human heads respond immediately to PQQ supplementation with variations in urinary metabolites constant with heightened mitochondria-related uses.