Electron transfer between a quinohemoprotein alcohol dehydrogenase and an electrode via a redox polymer network

Stigter, E.C.A.; Jong, Govardus A.H. de; Jongejan, Jaap A.; Duine, Johannis A.; Lugt, J.P. van der; Somers, W.

doi:10.1016/0141-0229(95)00158-1

Cited by 12 publications

(4 citation statements)

References 17 publications

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“…It was previously reported that the quinohemoprotein ADHs isolated from C. testosteroni, Acetobacter pasteurianus, and Acetobacter aceti exhibited an enantiomeric preference if racemic mixtures of chiral alcohols were used as substrates (15,17,29,30,43,44). Thus, we examined if THFA-DH from R. eutropha strain Bo also showed a preference for one enantiomer of different chiral alcohols.…”

Section: Resultsmentioning

confidence: 99%

Catalytic and Molecular Properties of the Quinohemoprotein Tetrahydrofurfuryl Alcohol Dehydrogenase from Ralstonia eutropha Strain Bo

2001

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The quinohemoprotein tetrahydrofurfuryl alcohol dehydrogenase (THFA-DH) from Ralstonia eutropha strain Bo was investigated for its catalytic properties. The apparent k cat /K m and K i values for several substrates were determined using ferricyanide as an artificial electron acceptor. The highest catalytic efficiency was obtained with n-pentanol exhibiting a k cat /K m value of 788 ؋ 10 4 M ؊1 s ؊1 . The enzyme showed substrate inhibition kinetics for most of the alcohols and aldehydes investigated. A stereoselective oxidation of chiral alcohols with a varying enantiomeric preference was observed. Initial rate studies using ethanol and acetaldehyde as substrates revealed that a ping-pong mechanism can be assumed for in vitro catalysis of THFA-DH. The gene encoding THFA-DH from R. eutropha strain Bo (tfaA) has been cloned and sequenced. The derived amino acid sequence showed an identity of up to 67% to the sequence of various quinoprotein and quinohemoprotein dehydrogenases. A comparison of the deduced sequence with the N-terminal amino acid sequence previously determined by Edman degradation analysis suggested the presence of a signal sequence of 27 residues. The primary structure of TfaA indicated that the protein has a tertiary structure quite similar to those of other quinoprotein dehydrogenases.

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Section: Resultsmentioning

confidence: 99%

Catalytic and Molecular Properties of the Quinohemoprotein Tetrahydrofurfuryl Alcohol Dehydrogenase from Ralstonia eutropha Strain Bo

2001

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“…Although this can be circumvented by using cells with higher aldehyde dehydrogenase content (the aldehyde forms are more inhibitory than the alcohol forms), this is only partial, so that further research is necessary before practical applications can be expected. One option could be the use of enzymes such as those embedded in a gel of electron‐conducting polymers, with electrochemical regeneration 31…”

Section: Applicationsmentioning

confidence: 99%

Cofactor diversity in biological oxidations: Implications and applications

Duine

2001

Chem. Record

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Until recently, it was generally believed that enzymatic oxidation and reduction requires the participation of either a nicotinamide (NAD(P)+) or a flavin (FAD, FMN), in agreement with the existence of NAD(P)/H-dependent dehydrogenases/reductases and flavoprotein dehydrogenases/reductases/oxidases. However, during the past 20 years, the unraveling of the enzymology of the oxidation and reduction of C1-compounds by bacteria has led to the discovery of many new redox cofactors, some of them discussed here as they have a wider physiological significance than just enabling enzymatic C1-conversions to occur. A good example is the quinone cofactors, encompassing PQQ (2,7,9-tricarboxy-1H-pyrrolo[2,3-f]-quinoline-4,5-dione), TTQ (tryptophyl tryptophanquinone), TPQ (topaquinone), LTQ (lysyl topaquinone), and several others whose structures have still to be elucidated. Another example is mycothiol (1-O-(2'-[N-acetyl-L-cysteinyl]amido-2'-deoxy-alpha-D-glucopyranosyl)-D-myo-inosoitol), the counterpart of glutathione, once thought to be a universal coenzyme. Because these novel cofactors assist in reactions that can also be catalyzed by already known enzyme "classic cofactor" combinations, and first indications suggest that the chemistry of the reactions is not unique, one may wonder about the evolutionary background for this cofactor diversity. However, as will be illustrated by examples, from a practical point of view the diversity is beneficial, as it has increased the arsenal of enzymes suitable for application.

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“…A third class of alcohol dehydrogenases, pyrroloquinoline quinone (PQQ) dependent alcohol dehydrogenases (EC1.1.99.8), has also been employed in biosensor designs for ethanol [18][19][20][21][22][23][24][25][26][27][28][29][30]. In contrast, methanol dehydrogenase (MDH) from which PQQ was first purified [31] has been rarely used in sensing applications [27,32].…”

Section: Introductionmentioning

confidence: 99%

Amperometric detection of methanol with a methanol dehydrogenase modified electrode sensor

Liu

Kirchhoff

2007

Journal of Electroanalytical Chemistry

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Electron transfer between a quinohemoprotein alcohol dehydrogenase and an electrode via a redox polymer network

Cited by 12 publications

References 17 publications

Catalytic and Molecular Properties of the Quinohemoprotein Tetrahydrofurfuryl Alcohol Dehydrogenase from Ralstonia eutropha Strain Bo

Catalytic and Molecular Properties of the Quinohemoprotein Tetrahydrofurfuryl Alcohol Dehydrogenase from Ralstonia eutropha Strain Bo

Cofactor diversity in biological oxidations: Implications and applications

Amperometric detection of methanol with a methanol dehydrogenase modified electrode sensor

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