Bioelectrocatalysis at electrodes coated with alcohol dehydrogenase, a quinohemoprotein with heme c serving as a built-in mediator

Tokuji Ikeda, Daisuke Kobayashi, Fumio Matsushita, Takamasa Sagara, Katsumi Niki

Research output: Contribution to journalArticle

110 Citations (Scopus)

Abstract

Alcohol dehydrogenase (ADH), a bacterial membrane-bound protein containing pyrroloquinoline quinone (PQQ) and heme c was held by adsorption on electrodes of gold, silver, glassy carbon, or pyrolytic graphite. All the electrodes with adsorbed ADH produced anodic currents which oxidized ethanol, in which the adsorbed ADH catalysed the electrolysis of ethanol. The electrocatalysis behavior could be described by a theoretical equation for bioelectrocatalysis at an enzyme-coated electrode, and was characterized by two quantities, the Michaelis constant Km, and maximum current density Imax/A. Using electroreflectance measurements with an ADH-coated gold electrode it was revealed that electron transfer occurred between heme c of the adsorbed ADH and the electrode. On the basis of these results, the reaction mechanism of the bioelectrocatalysis is discussed and oriented adsorption of ADH is proposed with the heme c moiety being in close contact with the electrode and with the PQQ moiety, the site reacting with the substrate, facing toward the solution.

Original languageEnglish
Pages (from-to)221-228
Number of pages8
JournalJournal of Electroanalytical Chemistry
Volume361
Issue number1-2
DOIs
Publication statusPublished - 15-12-1993

Fingerprint

Alcohol Dehydrogenase
Heme
Alcohols
Electrodes
PQQ Cofactor
Gold
Ethanol
Adsorption
Electrocatalysis
Graphite
Glassy carbon
Electrolysis
Silver
Oxidoreductases
Current density
Enzymes
Proteins
Membranes
Electrons
Substrates

All Science Journal Classification (ASJC) codes

  • Analytical Chemistry
  • Chemical Engineering(all)
  • Electrochemistry

Cite this

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title = "Bioelectrocatalysis at electrodes coated with alcohol dehydrogenase, a quinohemoprotein with heme c serving as a built-in mediator",
abstract = "Alcohol dehydrogenase (ADH), a bacterial membrane-bound protein containing pyrroloquinoline quinone (PQQ) and heme c was held by adsorption on electrodes of gold, silver, glassy carbon, or pyrolytic graphite. All the electrodes with adsorbed ADH produced anodic currents which oxidized ethanol, in which the adsorbed ADH catalysed the electrolysis of ethanol. The electrocatalysis behavior could be described by a theoretical equation for bioelectrocatalysis at an enzyme-coated electrode, and was characterized by two quantities, the Michaelis constant Km, and maximum current density Imax/A. Using electroreflectance measurements with an ADH-coated gold electrode it was revealed that electron transfer occurred between heme c of the adsorbed ADH and the electrode. On the basis of these results, the reaction mechanism of the bioelectrocatalysis is discussed and oriented adsorption of ADH is proposed with the heme c moiety being in close contact with the electrode and with the PQQ moiety, the site reacting with the substrate, facing toward the solution.",
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Bioelectrocatalysis at electrodes coated with alcohol dehydrogenase, a quinohemoprotein with heme c serving as a built-in mediator. / Ikeda, Tokuji; Kobayashi, Daisuke; Matsushita, Fumio; Sagara, Takamasa; Niki, Katsumi.

In: Journal of Electroanalytical Chemistry, Vol. 361, No. 1-2, 15.12.1993, p. 221-228.

Research output: Contribution to journalArticle

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T1 - Bioelectrocatalysis at electrodes coated with alcohol dehydrogenase, a quinohemoprotein with heme c serving as a built-in mediator

AU - Ikeda, Tokuji

AU - Kobayashi, Daisuke

AU - Matsushita, Fumio

AU - Sagara, Takamasa

AU - Niki, Katsumi

PY - 1993/12/15

Y1 - 1993/12/15

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AB - Alcohol dehydrogenase (ADH), a bacterial membrane-bound protein containing pyrroloquinoline quinone (PQQ) and heme c was held by adsorption on electrodes of gold, silver, glassy carbon, or pyrolytic graphite. All the electrodes with adsorbed ADH produced anodic currents which oxidized ethanol, in which the adsorbed ADH catalysed the electrolysis of ethanol. The electrocatalysis behavior could be described by a theoretical equation for bioelectrocatalysis at an enzyme-coated electrode, and was characterized by two quantities, the Michaelis constant Km, and maximum current density Imax/A. Using electroreflectance measurements with an ADH-coated gold electrode it was revealed that electron transfer occurred between heme c of the adsorbed ADH and the electrode. On the basis of these results, the reaction mechanism of the bioelectrocatalysis is discussed and oriented adsorption of ADH is proposed with the heme c moiety being in close contact with the electrode and with the PQQ moiety, the site reacting with the substrate, facing toward the solution.

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