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231224s2012 xx |||||o 00| ||eng c |
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|a 10.1021/la3005486
|2 doi
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|a pubmed24n0722.xml
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|a DE-627
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|e rakwb
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|a eng
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|a Harreither, Wolfgang
|e verfasserin
|4 aut
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|a Investigation of the pH-dependent electron transfer mechanism of ascomycetous class II cellobiose dehydrogenases on electrodes
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|c 2012
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|a Text
|b txt
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|a ƒaComputermedien
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|2 rdamedia
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|a ƒa Online-Ressource
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|2 rdacarrier
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|a Date Completed 18.09.2014
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|a Date Revised 04.02.2014
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Cellobiose dehydrogenase (CDH) is capable of direct electron transfer (DET) on various carbon and thiol-modified gold electrodes. As a result, these systems have been utilized as biocatalyst in biosensors and biofuel cell anodes. Class I CDHs, from basidiomycetous fungi, are highly specific to cellulose or lactose, and DET is only observed at pH values below 5.5. To extend the applicability of CDH-based electrodes, the catalytic properties and the behavior on electrode surfaces of ascomycetous class II CDHs from Chaetomium attrobrunneum, Corynascus thermophilus, Dichomera saubinetii, Hypoxylon haematostroma, Neurospora crassa, and Stachybotrys bisbyi were investigated. We found that class II CDHs have diverse properties but generally show a lower substrate specificity than class I CDHs by converting also glucose and maltose. Intramolecular electron transfer (IET) and DET at neutral and alkaline pH were observed and elucidated by steady-state kinetics, pre-steady-state kinetics, and electrochemical measurements. The CDHs ability to interact with the electron acceptor cytochrome c and to communicate with electrode surfaces through DET at various pH conditions was used to classify the investigated enzymes. In combination with stopped-flow measurements, a model for the kinetics of the pH-dependent IET is developed. The efficient glucose turnover at neutral/alkaline pH makes some of these new CDHs potential candidates for glucose biosensors and biofuel cell anodes
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Carbohydrate Dehydrogenases
|2 NLM
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|a EC 1.1.-
|2 NLM
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|a cellobiose-quinone oxidoreductase
|2 NLM
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|a EC 1.1.99.18
|2 NLM
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|a Nicholls, Peter
|e verfasserin
|4 aut
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|a Sygmund, Christoph
|e verfasserin
|4 aut
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|a Gorton, Lo
|e verfasserin
|4 aut
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| 700 |
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|a Ludwig, Roland
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1992
|g 28(2012), 16 vom: 24. Apr., Seite 6714-23
|w (DE-627)NLM098181009
|x 1520-5827
|7 nnns
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| 773 |
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|g volume:28
|g year:2012
|g number:16
|g day:24
|g month:04
|g pages:6714-23
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|u http://dx.doi.org/10.1021/la3005486
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