Literature DB >> 6250827

Structure and activity of the prosthetic group of methanol dehydrogenase.

J A Duine, J Frank, P E Verwiel.   

Abstract

The reconstructive ability of the isolated prosthetic group of methanol dehydrogenase with the apoenzyme of glucose dehydrogenase and the results of electron spin resonance measurements suggest that the prosthetic group has not been modified during the isolation. This result, and the properties of the directly isolated prosthetic group and derivatives, confirm the suggestion that its structure is 2,7,9-tricarboxy-1H-pyrrolo[2,3-f]quinoline-4,5-dione. From the activity shown by derivatives of the prosthetic group and of structural analogues in the apoenzyme test it is concluded that the o-quinone structure is essential for activity. Hence the trivial name pyrrolo-quinoline quinone would be appropriate. The testing of the analogues also shows that the pyrrolo ring and the 9-carboxylic acid group are not essential for activity as they can be replaced by a pyridinol ring and a 9-hydroxy group respectively. The determination of the molar absorption coefficient of the prosthetic group (18 400 M-1 cm-1 at 249 nm) enables its quantitative anaysis. Thus it could be established that methanol dehydrogenase contains one prosthetic group per enzyme molecule. The consequences of this result in relation to already known properties of this 'quinoprotein' dehydrogenase are discussed.

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Year:  1980        PMID: 6250827     DOI: 10.1111/j.1432-1033.1980.tb04711.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN: 0014-2956


  31 in total

1.  Two Different Quinohemoprotein Amine Dehydrogenases Initiate Anaerobic Degradation of Aromatic Amines in Aromatoleum aromaticum EbN1.

Authors:  Georg Schmitt; Martin Saft; Fabian Arndt; Jörg Kahnt; Johann Heider
Journal:  J Bacteriol       Date:  2019-07-24       Impact factor: 3.490

2.  Conformation of coenzyme pyrroloquinoline quinone and role of Ca2+ in the catalytic mechanism of quinoprotein methanol dehydrogenase.

Authors:  Y J Zheng; T C Bruice
Journal:  Proc Natl Acad Sci U S A       Date:  1997-10-28       Impact factor: 11.205

Review 3.  The three-subunit cytochrome bc1 complex of Paracoccus denitrificans. Its physiological function, structure, and mechanism of electron transfer and energy transduction.

Authors:  B L Trumpower
Journal:  J Bioenerg Biomembr       Date:  1991-04       Impact factor: 2.945

Review 4.  Metabolic pathways in Paracoccus denitrificans and closely related bacteria in relation to the phylogeny of prokaryotes.

Authors:  A H Stouthamer
Journal:  Antonie Van Leeuwenhoek       Date:  1992-01       Impact factor: 2.271

5.  Evidence for a chemiosmotic model of dehalorespiration in Desulfomonile tiedjei DCB-1.

Authors:  T M Louie; W W Mohn
Journal:  J Bacteriol       Date:  1999-01       Impact factor: 3.490

Review 6.  Cytochrome bc1 complexes of microorganisms.

Authors:  B L Trumpower
Journal:  Microbiol Rev       Date:  1990-06

Review 7.  PQQ and quinoproteins: an important novel field in enzymology.

Authors:  J A Duine
Journal:  Antonie Van Leeuwenhoek       Date:  1989-05       Impact factor: 2.271

8.  Effects of growth rate and oxygen tension on glucose dehydrogenase activity in Acinetobacter calcoaceticus LMD 79.41.

Authors:  B J van Schie; J P van Dijken; J G Kuenen
Journal:  Antonie Van Leeuwenhoek       Date:  1989       Impact factor: 2.271

9.  Cloning of the genes involved in synthesis of coenzyme pyrrolo-quinoline-quinone from Acinetobacter calcoaceticus.

Authors:  N Goosen; D A Vermaas; P van de Putte
Journal:  J Bacteriol       Date:  1987-01       Impact factor: 3.490

10.  Quinohaemoprotein alcohol dehydrogenase apoenzyme from Pseudomonas testosteroni.

Authors:  B W Groen; M A van Kleef; J A Duine
Journal:  Biochem J       Date:  1986-03-15       Impact factor: 3.857

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