Quinoproteins: structure, function, and biotechnological applications

Abstract. A new class of oxidoreductase containing an amino acid-derived o-quinone cofactor, of which the most typical is pyrroloquinoline quinone (PQQ), is called quinoproteins, and has been recognized as the third redox enzyme following pyridine nucleotide- and flavin-dependent dehydrogenases. Some quinoproteins include a heme c moiety in addition to the quinone cofactor in the molecule and are called quinohemoproteins. PQQ-containing quinoproteins and quinohemoproteins have a common structural basis, in which PQQ is deeply embedded in the center of the unique superbarrel structure. Increased evidence for the structure and function of quinoproteins has revealed their unique position within the redox enzymes with respect to catalytic and electron transfer properties, and also to physiological and energetic function. The peculiarities of the quinoproteins, together with their unique substrate specificity, have encouraged their biotechnological application in the fields of biosensing and bioconversion of useful compounds, and also to environmental treatment.

[1]  H. Rodríguez,et al.  Expression of a mineral phosphate solubilizing gene from Erwinia herbicola in two rhizobacterial strains. , 2000, Journal of biotechnology.

[2]  V. Davidson,et al.  Electron transfer reactions between aromatic amine dehydrogenase and azurin. , 1995, Biochemistry.

[3]  Takamasa Sagara,et al.  Bioelectrocatalysis at electrodes coated with alcohol dehydrogenase, a quinohemoprotein with heme c serving as a built-in mediator. , 1993 .

[4]  M. Yamada,et al.  C-terminal Periplasmic Domain of Escherichia coliQuinoprotein Glucose Dehydrogenase Transfers Electrons to Ubiquinone* , 2001, The Journal of Biological Chemistry.

[5]  S. Rhee,et al.  Purification of a membrane‐bound sorbitol dehydrogenase from Gluconobacter suboxydans , 1995 .

[6]  Braverman,et al.  Evidence for mutualism between a plant growing in a phosphate-limited desert environment and a mineral phosphate solubilizing (MPS) rhizobacterium. , 1999, FEMS microbiology ecology.

[7]  H. Izu,et al.  Functions of Amino Acid Residues in the Active Site ofEscherichia coli Pyrroloquinoline Quinone-Containing Quinoprotein Glucose Dehydrogenase* , 2000, The Journal of Biological Chemistry.

[8]  J. Jongejan,et al.  Enantioselective Conversions of the Racemic C3-Alcohol Synthons, Glycidol (2, 3-Epoxy-1-propanol), and Solketal (2, 2-Dimethyl-4-(hydroxymethyl)-1, 3-dioxolane) by Quinohaemoprotein Alcohol Dehydrogenases and Bacteria Containing Such Enzymes , 1994 .

[9]  Igarashi,et al.  Increasing the thermal stability of the water-soluble pyrroloquinoline quinone glucose dehydrogenase by single amino acid replacement. , 2000, Enzyme and microbial technology.

[10]  T. Hoshino,et al.  Purification and Properties of Membrane-bound D-Sorbitol Dehydrogenase from Gluconobacter suboxydans IFO 3255 , 2002, Bioscience, biotechnology, and biochemistry.

[11]  D. Hopper,et al.  Redox potential of the haem c group in the quinocytochrome, lupanine hydroxylase, an enzyme located in the periplasm of a Pseudomonas sp. , 1998, Biochimica et biophysica acta.

[12]  C. Anthony,et al.  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. , 1999, The Biochemical journal.

[13]  K. Matsushita,et al.  Electron transfer from quinohemoprotein alcohol dehydrogenase to blue copper protein azurin in the alcohol oxidase respiratory chain of Pseudomonas putida HK5. , 1999, Biochemistry.

[14]  K. Matsushita,et al.  Membrane-bound Quinoprotein D-Arabitol Dehydrogenase of Gluconobacter suboxydans IFO 3257: A Versatile Enzyme for the Oxidative Fermentation of Various Ketoses , 2001, Bioscience, biotechnology, and biochemistry.

[15]  K. Matsushita,et al.  Three distinct quinoprotein alcohol dehydrogenases are expressed when Pseudomonas putida is grown on different alcohols , 1995, Journal of bacteriology.

[16]  M. Yasuda,et al.  Polyethylene glycol dehydrogenase activity of Rhodopseudomonas acidophila derives from a type I quinohaemoprotein alcohol dehydrogenase , 1996 .

[17]  H. Yoshida,et al.  Construction and characterization of mutant water-soluble PQQ glucose dehydrogenases with altered K(m) values--site-directed mutagenesis studies on the putative active site. , 1999, Biochemical and biophysical research communications.

[18]  K. H. Kalk,et al.  Structure and mechanism of soluble quinoprotein glucose dehydrogenase , 1999, The EMBO journal.

[19]  J. Andreesen,et al.  Catalytic and Molecular Properties of the Quinohemoprotein Tetrahydrofurfuryl Alcohol Dehydrogenase from Ralstonia eutropha Strain Bo , 2001, Journal of bacteriology.

[20]  K. Sode,et al.  Extended-range glucose sensor employing engineered glucose dehydrogenases. , 2000, Analytical chemistry.

[21]  Taro Miyazaki,et al.  Molecular cloning and functional expression of D-sorbitol dehydrogenase from Gluconobacter suboxydans IF03255, which requires pyrroloquinoline quinone and hydrophobic protein SldB for activity development in E. coli. , 2002, Bioscience, biotechnology, and biochemistry.

[22]  A. Turner,et al.  Amperometric detection of histamine at a quinoprotein dehydrogenase enzyme electrode. , 1995, Biosensors & bioelectronics.

[23]  M. Shimao,et al.  Existence of a novel enzyme, pyrroloquinoline quinone-dependent polyvinyl alcohol dehydrogenase, in a bacterial symbiont, Pseudomonas sp. strain VM15C , 1986, Applied and environmental microbiology.

[24]  H. Iwamura,et al.  Topographical characterization of the ubiquinone reduction site of glucose dehydrogenase in Escherichia coli using depth-dependent fluorescent inhibitors. , 1999, Biochimica et biophysica acta.

[25]  A. Turner,et al.  Quinoprotein glucose dehydrogenase and its application in an amperometric glucose sensor. , 1986, Biosensors.

[26]  J. V. D. Lugt,et al.  Enantioselective oxidation of secondary alcohols at a quinohaemoprotein alcohol dehydrogenase electrode , 1998 .

[27]  K. Matsushita,et al.  Characterization of Quinohemoprotein Amine Dehydrogenase from Pseudomonas putida. , 1998, Bioscience, biotechnology, and biochemistry.

[28]  J. Duine,et al.  Quinohaemoprotein alcohol dehydrogenase apoenzyme from Pseudomonas testosteroni. , 1986, The Biochemical journal.

[29]  K. Kano,et al.  Biochemical and electrochemical characterization of quinohemoprotein amine dehydrogenase from Paracoccus denitrificans. , 1999, Biochemistry.

[30]  Adachi,et al.  Intramolecular electron transport in quinoprotein alcohol dehydrogenase of Acetobacter methanolicus: a redox-titration study , 1998, Biochimica et biophysica acta.

[31]  K. Watanabe,et al.  Increased production of recombinant pyrroloquinoline quinone (PQQ) glucose dehydrogenase by metabolically engineered Escherichia coli strain capable of PQQ biosynthesis. , 1996, Journal of biotechnology.

[32]  C. Anthony,et al.  The biochemistry, physiology and genetics of PQQ and PQQ-containing enzymes. , 1998, Advances in microbial physiology.

[33]  A. Straathof,et al.  Characterization of the Enantioselective Properties of the Quinohemoprotein Alcohol Dehydrogenase of Acetobacter pasteurianus LMG 1635. 1. Different Enantiomeric Ratios of Whole Cells and Purified Enzyme in the Kinetic Resolution of Racemic Glycidol. , 1999, Bioscience, biotechnology, and biochemistry.

[34]  W. Schuhmann,et al.  Polypyrrole-entrapped quinohemoprotein alcohol dehydrogenase. Evidence for direct electron transfer via conducting-polymer chains. , 1999, Analytical chemistry.

[35]  K. Matsushita,et al.  Function of Multiple Heme c Moieties in Intramolecular Electron Transport and Ubiquinone Reduction in the Quinohemoprotein Alcohol Dehydrogenase-Cytochrome c Complex of Gluconobacter suboxydans(*) , 1996, The Journal of Biological Chemistry.

[36]  A. Diehl,et al.  X-ray structure of the quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa: basis of substrate specificity. , 2000, Journal of molecular biology.

[37]  R. C. Siegel.  Lysyl oxidase. , 1979, International review of connective tissue research.

[38]  Y. Yamada,et al.  Topological analysis of quinoprotein glucose dehydrogenase in Escherichia coli and its ubiquinone-binding site. , 1993, The Journal of biological chemistry.

[39]  K. Matsushita,et al.  Respiratory chains and bioenergetics of acetic acid bacteria. , 1994, Advances in microbial physiology.

[40]  T. Hoshino,et al.  Isolation and Characterization of a New Quinoprotein Dehydrogenase, L-Sorbose/L-Sorbosone Dehydrogenase. , 1999, Bioscience, biotechnology, and biochemistry.