Probing redox reactions of immobilized cytochrome c using evanescent wave cavity ring-down spectroscopy in a thin-layer electrochemical cell.
Probing redox reactions of immobilized cytochrome c using evanescent wave cavity ring-down spectroscopy in a thin-layer electrochemical cell.
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在薄层电化学电池中使用倏逝波腔衰荡光谱法探测固定化细胞色素 c 的氧化还原反应。
DOI:
10.1002/cphc.201000213
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发表时间:
2010
期刊:
影响因子:
--
通讯作者:
Powell HV
中科院分区:
文献类型:
--
作者:
Powell HV
Electron transfer (ET) is fundamental to many biological processes. In particular, respiration and photosynthesis comprise a cascade of ET events involving redox proteins to produce energy in the cell.[1] Determining the rates of these processes, and the mechanisms that drive them, is important for understanding metabolic pathways in vivo. Furthermore, knowledge of ET to redox proteins is fundamental to optimizing technologies such as biosensors,[2, 3] biofuel cells,[4] heterogeneous catalysts [5] and biomolecular electronic components.[6] Traditionally, obtaining the kinetics of ET between proteins and redox mediators or other proteins was achieved in homogeneous solution using stopped flow apparatus and monitoring the change in the redox state of the protein by absorption spectroscopy.[7–11] However, since the first successful demonstrations of cyclic voltammetry of horse heart cytochrome c by Eddowes and Hill [12] and Yeh and Kuwana [13] independently in 1977, the area of the direct and mediated electrochemistry of both ET proteins and complex enzymes has flourished.[2, 14] Protein film voltammetry (PFV)[15] is widely accepted as a powerful tool for understanding ET between proteins and electrodes for the fabrication of devices such as biosensors,[2, 16] in bioelectronics and biofuel cells,[8, 9] and as a model approach for comprehending ET between redox proteins in vivo.[17] In PFV, a potential applied at an electrode drives electrons in and out of the active sites of an electroactive protein film immobilized on the electrode, allowing the evaluation of the formal potentials and the rates of ET and other kinetic and thermodynamic parameters.[18] Moreover, PFV has been employed to investigate the mechanisms and rates of ET between the adsorbed proteins and their redox partners.[19] Compared to homogeneous phase measurements, this was an important development because in vivo, ET often occurs at interfaces. Although PFV has been very successful in exploring many of these processes, it is limited due to the difficulty of orienting the protein in the film in such a way that it can undergo fast ET with the electrode and also dock successfully with its redox partners.Scanning electrochemical microscopy (SECM)[20] has also proved powerful in studying the redox properties of immobilized enzymes, including cytochrome c,[10] glucose oxidase,[21] and horse radish peroxidase.[22] Imaging of patterns of surfaceimmobilized enzymes using SECM is important to the characterization and optimization of enzyme-based sensors [23] and for the formation of biosensors, for example, for the detection of breast cancer markers.[24] An attraction of the SECM approach is that the enzymes do not have to be immobilized on an electrode surface, although they may be,[10a] thereby allowing ET kinetics to be investigated in a range of interfacial environ-
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影响因子:
3.9
作者:
T. Wilhelm;G. Wittstock
通讯作者:
G. Wittstock
DOI:
--
发表时间:
1978
期刊:
影响因子:
--
作者:
R. Holwerda;R. A. Read;R. A. Scott;S. Wherland;H. Gray;F. Millett
通讯作者:
F. Millett
DOI:
--
发表时间:
2004
期刊:
影响因子:
--
作者:
Hana Hoffmannová;D. Fermín;P. Krtil
通讯作者:
P. Krtil
DOI:
--
发表时间:
1974
期刊:
影响因子:
--
作者:
Hodges Hl;R. Holwerda;H. Gray
通讯作者:
H. Gray
影响因子:
--
作者:
Rocha MJ;Rocha E;Resende AD;Lobo-da-Cunha A
通讯作者:
Lobo-da-Cunha A