Pyrroloquinoline quinone

Jump to: navigation, search
Template:Chembox E number
Pyrroloquinoline quinone
ECHA InfoCard Lua error in Module:Wikidata at line 879: attempt to index field 'wikibase' (a nil value). Lua error in Module:Wikidata at line 879: attempt to index field 'wikibase' (a nil value).
MeSH PQQ+Cofactor
Molar mass 330.206 g/mol
Except where noted otherwise, data are given for
materials in their standard state
(at 25 °C, 100 kPa)

Infobox disclaimer and references

Pyrroloquinoline quinone (PQQ) was discovered by Houge as the third redox cofactor after nicotinamide and flavin in bacteria. [1]. Anthony and Zatman also found the unknown redox cofactor in alcohol dehydrogenase and named Metoxatin [2]. In 1979, Salisbury and colleagues [3] as well as Duine and colleagues [4] extracted this coenzyme from methanol dehydrogenase of methylotroph and identified its molecular structure. Adachi and colleagues identified that PQQ was also found in Acetobacter [5]. These enzymes containing PQQ are called quinoproteins. Glucose dehydrogenase, one of quinoproteins, is used for glucose sensor. Subsequently, PQQ was found to have the growth stimulation effect in bacteria [6]. In addition, antioxidant effect and neuroprotective effect were also found. In 1989, Rucker and colleagues reported that mice deprived of PQQ showed various abnormalities and it was suggested that PQQ might have an important nutritional role also in mammals [7]. In 2003, it was reported that aminoadipic semialdehyde dehydrogenase (AASDH) might also use PQQ as a cofactor, suggesting a possibility that PQQ is a vitamin in mammals [8]. However, there is no direct evidence that AASDH requires PQQ as a cofactor in its enzymatic activity. Rucker and colleagues concluded that insufficient information is available so far to state that PQQ is a vitamin for mammals, although PQQ may be an important biological factor [9].


  1. Hauge JG (1964). "Glucose dehydrogenase of bacterium anitratum: an enzyme with a novel prosthetic group". J Biol Chem. 239: 3630–9. PMID 14257587
  2. Anthony C, Zatman LJ (1967). "The microbial oxidation of methanol. The prosthetic group of the alcohol dehydrogenase of Pseudomonas sp. M27: a new oxidoreductase prosthetic group". Biochem J. 104 (3): 960–9. PMID 6049934
  3. Salisbury SA, Forrest HS, Cruse WB, Kennard O (1979). "A novel coenzyme from bacterial primary alcohol dehydrogenases". Nature. 280 (5725): 843–4. PMID 471057
  4. Westerling J, Frank J, Duine JA (1979). "The prosthetic group of methanol dehydrogenase from Hyphomicrobium X: electron spin resonance evidence for a quinone structure". Biochem Biophys Res Commun. 87 (3): 719–24. PMID 222269
  5. Ameyama M, Matsushita K, Ohno Y, Shinagawa E, Adachi O (1981). "Existence of a novel prosthetic group, PQQ, in membrane-bound, electron transport chain-linked, primary dehydrogenases of oxidative bacteria". FEBS Lett. 130 (2): 179–83. PMID 6793395
  6. Ameyama M, Matsushita K, Shinagawa E, Hayashi M, Adachi O (1988). "Pyrroloquinoline quinone: excretion by methylotrophs and growth stimulation for microorganisms". Biofactors. 1 (1): 51–3. PMID 2855583
  7. Killgore J, Smidt C, Duich L, Romero-Chapman N, Tinker D, Reiser K, Melko M, Hyde D, Rucker RB (1989). "Nutritional importance of pyrroloquinoline quinone". Science. 245 (4920): 850–2. PMID 2549636
  8. Kasahara T, Kato T (2003). "Nutritional biochemistry: A new redox-cofactor vitamin for mammals". Nature. 422 (6934): 832. PMID 12712191
  9. Rucker R, Storms D, Sheets A, Tchaparian E, Fascetti A (2005). "Biochemistry: is pyrroloquinoline quinone a vitamin?". Nature. 433 (7025): E10–1, discussion E11-2. PMID 15689994

External links