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231224s2012 xx |||||o 00| ||eng c |
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|a 10.1021/la3018858
|2 doi
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|a pubmed24n0730.xml
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|a (DE-627)NLM219043957
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|a (NLM)22746277
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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|a Matsumura, Hirotoshi
|e verfasserin
|4 aut
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| 245 |
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|a Direct electrochemistry of Phanerochaete chrysosporium cellobiose dehydrogenase covalently attached onto gold nanoparticle modified solid gold electrodes
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|c 2012
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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|a Date Completed 30.11.2012
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|a Date Revised 25.07.2012
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Achieving efficient electrochemical communication between redox enzymes and various electrode materials is one of the main challenges in bioelectrochemistry and is of great importance for developing electronic applications. Cellobiose dehydrogenase (CDH) is an extracellular flavocytochrome composed of a catalytic FAD containing dehydrogenase domain (DH(CDH)), a heme b containing cytochrome domain (CYT(CDH)), and a flexible linker region connecting the two domains. Efficient direct electron transfer (DET) of CDH from the basidiomycete Phanerochaete chrysosporium (PcCDH) covalently attached to mixed self-assembled monolayer (SAM) modified gold nanoparticle (AuNP) electrode is presented. The thiols used were as follows: 4-aminothiophenol (4-ATP), 4-mercaptobenzoic acid (4-MBA), 4-mercaptophenol (4-MP), 11-mercapto-1-undecanamine (MUNH(2)), 11-mercapto-1-undecanoic acid (MUCOOH), and 11-mercapto-1-undecanol (MUOH). A covalent linkage between PcCDH and 4-ATP or MUNH(2) in the mixed SAMs was formed using glutaraldehyde as cross-linker. The covalent immobilization and the surface coverage of PcCDH were confirmed with surface plasmon resonance (SPR). To improve current density, AuNPs were cast on the top of polycrystalline gold electrodes. For all the immobilized PcCDH modified AuNPs electrodes, cyclic voltammetry exhibited clear electrochemical responses of the CYT(CDH) with fast electron transfer (ET) rates in the absence of substrate (lactose), and the formal potential was evaluated to be +162 mV vs NHE at pH 4.50. The standard ET rate constant (k(s)) was estimated for the first time for CDH and was found to be 52.1, 59.8, 112, and 154 s(-1) for 4-ATP/4-MBA, 4-ATP/4-MP, MUNH(2)/MUCOOH, and MUNH(2)/MUOH modified electrodes, respectively. At all the mixed SAM modified AuNP electrodes, PcCDH showed DET only via the CYT(CDH). No DET communication between the DH(CDH) domain and the electrode was found. The current density for lactose oxidation was remarkably increased by introduction of the AuNPs. The 4-ATP/4-MBA modified AuNPs exhibited a current density up to 30 μA cm(-2), which is ∼70 times higher than that obtained for a 4-ATP/4-MBA modified polycrystalline gold electrode. The results provide insight into fundamental electrochemical properties of CDH covalently immobilized on gold electrodes and promote further applications of CDHs for biosensors, biofuel cells, and bioelectrocatalysis
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Enzymes, Immobilized
|2 NLM
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| 650 |
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|a Gold
|2 NLM
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| 650 |
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|a 7440-57-5
|2 NLM
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|a Carbohydrate Dehydrogenases
|2 NLM
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| 650 |
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|a EC 1.1.-
|2 NLM
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|a cellobiose-quinone oxidoreductase
|2 NLM
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| 650 |
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|a EC 1.1.99.18
|2 NLM
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| 700 |
1 |
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|a Ortiz, Roberto
|e verfasserin
|4 aut
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|a Ludwig, Roland
|e verfasserin
|4 aut
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| 700 |
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|a Igarashi, Kiyohiko
|e verfasserin
|4 aut
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| 700 |
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|a Samejima, Masahiro
|e verfasserin
|4 aut
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| 700 |
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|a Gorton, Lo
|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), 29 vom: 24. Juli, Seite 10925-33
|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:29
|g day:24
|g month:07
|g pages:10925-33
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|u http://dx.doi.org/10.1021/la3018858
|3 Volltext
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|h 10925-33
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