Enantioselective oxidation of secondary alcohols at a quinohaemoprotein alcohol dehydrogenase electrode

Somers, W.; Stigter, E.C.A.; Hartingsveldt, W. van; Lugt, J.P. van der

doi:10.1007/bf02787770

Cited by 9 publications

(6 citation statements)

References 21 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…On the other hand, C. testosteroni ADH II is able to oxidize racemic solketal with a very high preference for the R-enantiomer (E=117) to produce the S-solketal (Geerlof et al 1994). In the latter case, enantioselectivity has been confirmed even by electrochemical reaction in an enzyme-immobilized electrode (Somers et al 1998). …”

Section: Bioconversion Of Useful Materialsmentioning

confidence: 90%

“…Type II ADHs from Comamonas testosteroni and Ralstonia eutropha, and type III ADHs from acetic acid bacteria have been examined for their enantioselectivity. All these quinohemoprotein ADHs have a preference toward the S-form of secondary alcohols, in which the affinity for the S-enantiomer becomes more absolute with increased chain length (Geerlof et al 1994;Somers et al, 1998;Zarnt et al 2001). The enantioselectivity for the S(-)-secondary alcohol (E value) differs depending on the enzyme source; from E=310 for 2-hexanol in the case of ADH II of C. testosteroni to E=34 for 2-hexanol in ADH III of Acetobacter pasteurianus.…”

Section: Bioconversion Of Useful Materialsmentioning

confidence: 96%

See 1 more Smart Citation

Quinoproteins: structure, function, and biotechnological applications

Matsushita

Toyama

Yamada

et al. 2002

Applied Microbiology and Biotechnology

134

View full text Add to dashboard Cite

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.

show abstract

Section: Bioconversion Of Useful Materialsmentioning

confidence: 90%

Section: Bioconversion Of Useful Materialsmentioning

confidence: 96%

Quinoproteins: structure, function, and biotechnological applications

Matsushita

Toyama

Yamada

et al. 2002

Applied Microbiology and Biotechnology

134

View full text Add to dashboard Cite

show abstract

“…Other syntheses in which TBADH was used coupled to NADPH regeneration by a dehydrogenase were less successful [184][185][186], yielding 80% product and showing TTN values of not more than 10 [186].…”

Section: Enzymatic Syntheses Involving Alcoholsmentioning

confidence: 97%

Redox Enzymes Used in Chiral Syntheses Coupled to Coenzyme Regeneration

Leonida¹

2001

CMC

View full text Add to dashboard Cite

Due to their ability to perform reactions in a stereo- and regiospecific manner, while functioning under mild conditions of temperature and pH, enzymes are increasingly used for chiral synthesis in the pharmaceutical industry, in medicinal chemistry, agriculture, cosmetic and food industry. The oxidoreductases as catalysts require a coenzyme (cofactor) which functions as an electron carrier. If used in stoichiometric amounts the cost of coenzymes makes synthetic applications of redox enzymes prohibitively expensive for industrial applications. The present review updates previous discussions about the objectives of cofactor regeneration as a requirement for the applicability of enzymatic redox reactions, and about the strategies customarily used to this end. Different types of chiral syntheses coupled successfully to coenzyme regeneration (amino acid synthesis, lactone synthesis, synthetic reactions involving alcohols, hydroxy acid and steroid synthesis, deracemization) are then discussed. New catalysts, cross-linked enzyme crystals, prepared from redox enzyme are presented in a small paragraph together with some of their applications. Special attention is given to whole cells used in this type of synthesis and their advantages and disadvantages are presented in one paragraph. Finally, different reactors, within which were conducted chiral syntheses catalyzed by oxireductases and coupled to cofactor regeneration, are briefly discussed.

show abstract

“…The enantioselectivity increases with increasing chain length. The same enzyme was immobilized on the surface of electrode and used in that form for preparative purposes (Somers et al, 1998). Although another type of alcohol dehydrogenases were used for biosensor design (Jiang et al 2009) Quinohaemoprotein alcohol dehydrogenase as yet didn't find any analytical application.…”

Section: Chiral Catalysismentioning

confidence: 99%