Pyrroloquinoline quinone (PQQ) was discovered by J.G. Hauge as the third redox cofactor after nicotinamide and flavin in bacteria (although he hypothesised that it was naphthoquinone). Anthony and Zatman also found the unknown redox cofactor in alcohol dehydrogenase and named it methoxatin. Adachi and colleagues identified that PQQ was also found in Acetobacter.
These enzymes containing PQQ are called quinoproteins. Glucose dehydrogenase, one of the quinoproteins, is used as a glucose sensor. Subsequently, PQQ was found to stimulate growth in bacteria. In addition, antioxidant and neuroprotective effects were also found.
- Mitochondrial biogenesis in mice
- Cardioprotection in rat models
PQQ is a neuroprotective compound that has been shown in a small number of preliminary studies to protect memory and cognition in aging animals and humans. It has been shown to reverse cognitive impairment caused by chronic oxidative stress in animal models and improve performance on memory tests. PQQ supplementation stimulates the production and release of nerve growth factors in cells that support neurons in the brain, a possible mechanism for the improvement of memory function it appears to produce in aging humans and rats.
PQQ has also been shown to safeguard against the self-oxidation of the DJ-1 protein, an early step in the onset of some forms of Parkinson's disease.
PQQ protects brain cells against oxidative damage following ischemia-reperfusion injury—the inflammation and oxidative damage that result from the sudden return of blood and nutrients to tissues deprived of them by stroke. Reactive nitrogen species (RNS) arise spontaneously following stroke and spinal cord injuries and impose severe stresses on damaged neurons, contributing to subsequent long-term neurological damage. PQQ suppresses RNS in experimentally induced strokes, and provides additional protection following spinal cord injury by blocking inducible nitric oxide synthase (iNOS), a major source of RNS.
In animal models, administration of PQQ immediately prior to induction of stroke significantly reduces the size of the damaged brain area. These observations have been compounded by the observation in vivo that PQQ protects against the likelihood of severe stroke in an experimental animal model for stroke and brain hypoxia.
PQQ also affects some of the brain’s neurotransmitter systems. It protects neurons by modulating the properties of the N-methyl-D-aspartate (NMDA) receptor, and so reducing excitotoxicity—the damaging consequence of long-term overstimulation of neurons that is associated with many neurodegenerative diseases and seizures.
PQQ also protects the brain against neurotoxicity induced by other powerful toxins, including mercury(a suspected factor in the development of Alzheimer's disease) and oxidopamine (a potent neurotoxin used by scientists to induce Parkinsonism in laboratory animals by destroying dopaminergic and noradrenergic neurons.)
PQQ prevents aggregation of alpha-synuclein, a protein associated with Parkinson's disease. PQQ also protects nerve cells from the toxic effects of the amyloid-beta protein linked with Alzheimer's disease, and reduces the formation of new amyloid beta aggregates.
Dietary pyrroloquinoline quinone (PQQ) alters indicators of inflammation and mitochondrial-related metabolism in human subjects.
Existence of a novel prosthetic group, PQQ, in membrane-bound, electron transport chain-linked, primary dehydrogenases of oxidative bacteria.
L-Lysine plays a major role in calcium absorption; building muscle protein; recovering from surgery or sports injuries; and the body's production of hormones, enzymes, and antibodies.
Lysine is the limiting amino acid (the essential amino acid found in the smallest quantity in the particular foodstuff) in most cereal grains, but is plentiful in most pulses (legumes). Consequently, meals that combine cereal grains and legumes, such as the Indian dal with rice, Middle Eastern hummus, ful medames, falafel with pita bread, the Mexican beans with rice or tortilla have arisen to provide complete protein in diets that are, by choice or by necessity, vegetarian. A food is considered to have sufficient lysine if it has at least 51 mg of lysine per gram of protein (so that the protein is 5.1% lysine).
Histidine: "The enzyme histidine ammonia-lyase converts histidine into ammonia and urocanic acid. A deficiency in this enzyme is present in the rare metabolic disorder histidinemia. In Actinobacteria and filamentous fungi, such as Neurospora crassa, histidine can be converted into the antioxidant ergothioneine."