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Surface characterization and direct bioelectrocatalysis of multicopper oxidases
被引:46
作者:
Ivnitski, Dmitri M.
[1
,2
]
Khripin, Constantine
[1
]
Luckarift, Heather R.
[2
,3
]
Johnson, Glenn R.
[2
]
Atanassov, Plamen
[1
]
机构:
[1] Univ New Mexico, Albuquerque, NM 87131 USA
[2] USAF, Res Lab, AFRL RXQL Microbiol & Appl Biochem, Tyndall AFB, FL 32403 USA
[3] Universal Technol Corp, Dayton, OH 45432 USA
关键词:
Laccase;
Bilirubin oxidase;
Ascorbate oxidase;
Bio-cathode;
Enzymatic fuel cell;
DIRECT ELECTRON-TRANSFER;
RHUS-VERNICIFERA LACCASE;
TRAMETES-HIRSUTA LACCASE;
MODIFIED GOLD ELECTRODES;
ATOMIC-FORCE MICROSCOPY;
COPPER ACTIVE-SITE;
BILIRUBIN OXIDASE;
ASCORBATE OXIDASE;
BIOFUEL CELLS;
FUNGAL LACCASES;
D O I:
10.1016/j.electacta.2010.07.026
中图分类号:
O646 [电化学、电解、磁化学];
学科分类号:
081704 ;
摘要:
Multicopper oxidases (MCO) have been extensively studied as oxygen reduction catalysts for cathodic reactions in biofuel cells Theoretically. direct electron transfer between an enzyme and electrode offers optimal energy conversion efficiency providing that the enzyme/electrode interface can be engineered to establish efficient electrical communication. In this study, the direct bioelectrocatalysts of three MCO (Laccase from Trametes versicolor, bilirubin oxidase (BOD) from the fungi Myrothecium verrucaria and ascorbate oxidase(AOx) from Cucurbita sp.) was investigated and compared as oxygen reduction Protein film voltammetry and electrochemical characterization of the MCO electrodes showed that DET had been successfully established in all cases. Atomic force microscopy imaging and force measurements indicated that enzyme was immobilized as a monolayer on the electrode surface Evidence for three clearly separated anodic and cathodic redox events related to the Type 1 (T1) and the trinculear copper centers (T2, T3) of various MCO was observed. The redox potential of the T1 center was strongly modulated by physiological factors including pH, anaerobic and aerobic conditions and the presence of inhibitor S. (C) 2010 Elsevier Ltd All rights reserved.
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页码:7385 / 7393
页数:9
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