Spectroelectrochemical Characterization of Quinohemoprotein Alcohol Dehydrogenase from Gluconobacter suboxydans
- 1 June 1997
- journal article
- Published by Oxford University Press (OUP) in Chemistry Letters
- Vol. 26 (6) , 525-526
- https://doi.org/10.1246/cl.1997.525
Abstract
Direct electron transfer of alcohol dehydrogenase (ADH) from Gluconobacter suboxydans, which contains one pyrroloquinoline quinone (PQQ) and four hemes c, are realized on a carbon-wool column electrode. Potential-dependent spectral change monitored with a photodiode array detector is well explained by a five-step Nernstian electron transfer model. The evaluated redox potentials are reasonable to explain the chemical reactivity of ADH with various redox reagents.This publication has 6 references indexed in Scilit:
- Function of Multiple Heme c Moieties in Intramolecular Electron Transport and Ubiquinone Reduction in the Quinohemoprotein Alcohol Dehydrogenase-Cytochrome c Complex of Gluconobacter suboxydansPublished by Elsevier ,1996
- Bioelectrocatalysis by Alcohol Dehydrogenase from Aetobacter aceti Adsorbed on Bare and Chemically Modified ElectrodesDenki Kagaku oyobi Kogyo Butsuri Kagaku, 1994
- Bioelectrocatalysis at electrodes coated with alcohol dehydrogenase, a quinohemoprotein with heme c serving as a built-in mediatorJournal of Electroanalytical Chemistry, 1993
- Electrochemical Reduction of Cytochrome c by Using a Column-Electrolytic Continuous-Flow MethodDenki Kagaku oyobi Kogyo Butsuri Kagaku, 1993
- Analytical chemical study on actionoids ions by column electrolysis.BUNSEKI KAGAKU, 1991
- [76] Alcohol dehydrogenase from acetic acid bacteria, membrane-boundPublished by Elsevier ,1982