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Journal articles on the topic 'Electrochemistry of enzymes'

Author: Grafiati

Published: 4 June 2021

Last updated: 8 February 2022

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1

Bernhardt, Paul V. "Enzyme Electrochemistry — Biocatalysis on an Electrode." Australian Journal of Chemistry 59, no. 4 (2006): 233. http://dx.doi.org/10.1071/ch05340.

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Oxidoreductase enzymes catalyze single- or multi-electron reduction/oxidation reactions of small molecule inorganic or organic substrates, and they are integral to a wide variety of biological processes including respiration, energy production, biosynthesis, metabolism, and detoxification. All redox enzymes require a natural redox partner such as an electron-transfer protein (e.g. cytochrome, ferredoxin, flavoprotein) or a small molecule cosubstrate (e.g. NAD(P)H, dioxygen) to sustain catalysis, in effect to balance the substrate/product redox half-reaction. In principle, the natural electron-transfer partner may be replaced by an electrochemical working electrode. One of the great strengths of this approach is that the rate of catalysis (equivalent to the observed electrochemical current) may be probed as a function of applied potential through linear sweep and cyclic voltammetry, and insight to the overall catalytic mechanism may be gained by a systematic electrochemical study coupled with theoretical analysis. In this review, the various approaches to enzyme electrochemistry will be discussed, including direct and indirect (mediated) experiments, and a brief coverage of the theory relevant to these techniques will be presented. The importance of immobilizing enzymes on the electrode surface will be presented and the variety of ways that this may be done will be reviewed. The importance of chemical modification of the electrode surface in ensuring an environment conducive to a stable and active enzyme capable of functioning natively will be illustrated. Fundamental research into electrochemically driven enzyme catalysis has led to some remarkable practical applications. The glucose oxidase enzyme electrode is a spectacularly successful application of enzyme electrochemistry. Biosensors based on this technology are used worldwide by sufferers of diabetes to provide rapid and accurate analysis of blood glucose concentrations. Other applications of enzyme electrochemistry are in the sensing of macromolecular complexation events such as antigen–antibody binding and DNA hybridization. The review will include a selection of enzymes that have been successfully investigated by electrochemistry and, where appropriate, discuss their development towards practical biotechnological applications.

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2

Lin, Chuhong, Lior Sepunaru, Enno Kätelhön, and Richard G. Compton. "Electrochemistry of Single Enzymes: Fluctuations of Catalase Activities." Journal of Physical Chemistry Letters 9, no. 11 (May 11, 2018): 2814–17. http://dx.doi.org/10.1021/acs.jpclett.8b01199.

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3

GUO, L. H., and H. A. O. HILL. "ChemInform Abstract: Direct Electrochemistry of Proteins and Enzymes." ChemInform 22, no. 50 (August 22, 2010): no. http://dx.doi.org/10.1002/chin.199150345.

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4

Hill, H. A. O. "Making Use of the Direct Electrochemistry of Enzymes." Portugaliae Electrochimica Acta 19, no. 3 (2001): 165–70. http://dx.doi.org/10.4152/pea.200103165.

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5

Peterbauer, Clemens K. "Pyranose dehydrogenases: Rare enzymes for electrochemistry and biocatalysis." Bioelectrochemistry 132 (April 2020): 107399. http://dx.doi.org/10.1016/j.bioelechem.2019.107399.

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6

Davis, Connor, Stephanie X. Wang, and Lior Sepunaru. "What can electrochemistry tell us about individual enzymes?" Current Opinion in Electrochemistry 25 (February 2021): 100643. http://dx.doi.org/10.1016/j.coelec.2020.100643.

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7

Gulaboski, Rubin, and Valentin Mirceski. "Application of voltammetry in biomedicine - Recent achievements in enzymatic voltammetry." Macedonian Journal of Chemistry and Chemical Engineering 39, no. 2 (November 12, 2020): 153. http://dx.doi.org/10.20450/mjcce.2020.2152.

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Protein-film voltammetry (PFV) is considered the simplest methodology to study the electrochemistry of lipophilic redox enzymes in an aqueous environment. By anchoring particular redox enzymes on the working electrode surface, it is possible to get an insight into the mechanism of enzyme action. The PFV methodology enables access to the relevant thermodynamic and kinetic parameters of the enzyme-electrode reaction and enzyme-substrate interactions, which is important to better understand many metabolic pathways in living systems and to delineate the physiological role of enzymes. PFV additionally provides important information which is useful for designing specific biosensors, simple medical devices and bio-fuel cells. In the current review, we focus on some recent achievements of PFV, while presenting some novel protocols that contribute to a better communication between redox enzymes and the working electrode. Insights to several new theoretical models that provide a simple strategy for studying electrode reactions of immobilized enzymes and that enable both kinetic and thermodynamic characterization of enzyme-substrate interactions are also provided. In addition, we give a short overview to several novel voltammetric techniques, derived from the perspective of square-wave voltammetry, which seem to be promising tools for application in PFV.

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8

KASAI, Nahoko, Yasuhiko JIMBO, Osamu NIWA, Tomokazu MATSUE, and Keiichi TORIMITSU. "Multichannel Glutamate Monitoring by Electrode Array Electrochemically Immobilized with Enzymes." Electrochemistry 68, no. 11 (November 5, 2000): 886–89. http://dx.doi.org/10.5796/electrochemistry.68.886.

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9

Schachinger, Franziska, Hucheng Chang, Stefan Scheiblbrandner, and Roland Ludwig. "Amperometric Biosensors Based on Direct Electron Transfer Enzymes." Molecules 26, no. 15 (July 27, 2021): 4525. http://dx.doi.org/10.3390/molecules26154525.

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The accurate determination of analyte concentrations with selective, fast, and robust methods is the key for process control, product analysis, environmental compliance, and medical applications. Enzyme-based biosensors meet these requirements to a high degree and can be operated with simple, cost efficient, and easy to use devices. This review focuses on enzymes capable of direct electron transfer (DET) to electrodes and also the electrode materials which can enable or enhance the DET type bioelectrocatalysis. It presents amperometric biosensors for the quantification of important medical, technical, and environmental analytes and it carves out the requirements for enzymes and electrode materials in DET-based third generation biosensors. This review critically surveys enzymes and biosensors for which DET has been reported. Single- or multi-cofactor enzymes featuring copper centers, hemes, FAD, FMN, or PQQ as prosthetic groups as well as fusion enzymes are presented. Nanomaterials, nanostructured electrodes, chemical surface modifications, and protein immobilization strategies are reviewed for their ability to support direct electrochemistry of enzymes. The combination of both biosensor elements—enzymes and electrodes—is evaluated by comparison of substrate specificity, current density, sensitivity, and the range of detection.

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10

Shukla, Alka, Elizabeth M. Gillam, Deanne J. Mitchell, and Paul V. Bernhardt. "Direct electrochemistry of enzymes from the cytochrome P450 2C family." Electrochemistry Communications 7, no. 4 (April 2005): 437–42. http://dx.doi.org/10.1016/j.elecom.2005.02.021.

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11

Bernhardt, Paul V. "Exploiting the versatility and selectivity of Mo enzymes with electrochemistry." Chem. Commun. 47, no. 6 (2011): 1663–73. http://dx.doi.org/10.1039/c0cc03681a.

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12

Sorrentino, Ilaria, Ilaria Stanzione, Yannig Nedellec, Alessandra Piscitelli, Paola Giardina, and Alan Le Goff. "From Graphite to Laccase Biofunctionalized Few-Layer Graphene: A “One Pot” Approach Using a Chimeric Enzyme." International Journal of Molecular Sciences 21, no. 11 (May 26, 2020): 3741. http://dx.doi.org/10.3390/ijms21113741.

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A chimeric enzyme based on the genetic fusion of a laccase with a hydrophobin domain was employed to functionalize few-layer graphene, previously exfoliated from graphite in the presence of the hydrophobin. The as-produced, biofunctionalized few-layer graphene was characterized by electrochemistry and Raman spectroscopy, and finally employed in the biosensing of phenols such as catechol and dopamine. This strategy paves the way for the functionalization of nanomaterials by hydrophobin domains of chimeric enzymes and their use in a variety of electrochemical applications.

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13

Curulli, Antonella, and Daniela Zane. "Gold and Nanostructurated Surfaces for Assembling of Electrochemical Biosensors." Research Letters in Nanotechnology 2008 (2008): 1–4. http://dx.doi.org/10.1155/2008/789153.

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Devices based on nanomaterials are emerging as a powerful and general class of ultrasensitive sensors for the direct detection of biological and chemical species. In this work, we report the preparation and the full characterization of nanomaterials such as gold nanowires and nanostructured films to be used for assembling of electrochemical biosensors. Gold nanowires were prepared by electroless deposition within the pores of polycarbonate particle track-etched membranes (PTMs). Glucose oxidase was deposited onto the nanowires using self-assembling monolayer as an anchor layer for the enzyme molecules. Finally, cyclic voltammetry was performed for different enzymes to test the applicability of gold nanowires as biosensors. Considering another interesting nanomaterial, the realization of functionalised thin films on Si substrates for the immobilization of enzymes is reported. Glucose oxidase and horseradish peroxidase immobilized onto -based nanostructured surfaces exhibited a pair of well-defined and quasireversible voltammetric peaks. The electron exchange between the enzyme and the electrodes was greatly enhanced in the nanostructured environment. The electrocatalytic activity of HRP and GOD embedded in electrodes toward and glucose, respectively, may have a potential perspective in the fabrication of third-generation biosensors based on direct electrochemistry of enzymes.

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14

Yin, Yajing, Yafen Lü, Ping Wu, and Chenxin Cai. "Direct Electrochemistry of Redox Proteins and Enzymes Promoted by Carbon Nanotubes." Sensors 5, no. 4 (April 27, 2005): 220–34. http://dx.doi.org/10.3390/s5040220.

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15

Léger, Christophe, and Patrick Bertrand. "Direct Electrochemistry of Redox Enzymes as a Tool for Mechanistic Studies." Chemical Reviews 108, no. 7 (July 2008): 2379–438. http://dx.doi.org/10.1021/cr0680742.

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16

Sun, Dongmei, Chenxin Cai, Wei Xing, and Tianhong Lu. "Immobilization and direct electrochemistry of copper-containing enzymes on active carbon." Chinese Science Bulletin 49, no. 23 (December 2004): 2452–54. http://dx.doi.org/10.1007/bf03183712.

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17

OYAMATSU, Daisuke, Norihiro KANAYA, Yu HIRANO, Matsuhiko NISHIZAWA, and Tomokazu MATSUE. "Area-selective Immobilization of Multi Enzymes by Using the Reductive Desorption of Self-assembled Monolayer." Electrochemistry 71, no. 6 (June 5, 2003): 439–41. http://dx.doi.org/10.5796/electrochemistry.71.439.

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18

Chirkov, Yu G., and V. I. Rostokin. "Porous Electrodes with Immobilized Enzymes: The Problem of Development of Nanocomposites with High Concentrations of Molecules of Active Enzymes." Russian Journal of Electrochemistry 41, no. 11 (November 2005): 1221–30. http://dx.doi.org/10.1007/s11175-005-0206-9.

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19

Addo, Paul K, Robert L Arechederra, and Shelley D Minteer. "Evaluating Enzyme Cascades for Methanol/Air Biofuel Cells Based on NAD+-Dependent Enzymes." Electroanalysis 22, no. 7-8 (March 24, 2010): 807–12. http://dx.doi.org/10.1002/elan.200980009.

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20

Hitaishi, Vivek, Romain Clement, Nicolas Bourassin, Marc Baaden, Anne De Poulpiquet, Sophie Sacquin-Mora, Alexandre Ciaccafava, and Elisabeth Lojou. "Controlling Redox Enzyme Orientation at Planar Electrodes." Catalysts 8, no. 5 (May 4, 2018): 192. http://dx.doi.org/10.3390/catal8050192.

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Redox enzymes, which catalyze reactions involving electron transfers in living organisms, are very promising components of biotechnological devices, and can be envisioned for sensing applications as well as for energy conversion. In this context, one of the most significant challenges is to achieve efficient direct electron transfer by tunneling between enzymes and conductive surfaces. Based on various examples of bioelectrochemical studies described in the recent literature, this review discusses the issue of enzyme immobilization at planar electrode interfaces. The fundamental importance of controlling enzyme orientation, how to obtain such orientation, and how it can be verified experimentally or by modeling are the three main directions explored. Since redox enzymes are sizable proteins with anisotropic properties, achieving their functional immobilization requires a specific and controlled orientation on the electrode surface. All the factors influenced by this orientation are described, ranging from electronic conductivity to efficiency of substrate supply. The specificities of the enzymatic molecule, surface properties, and dipole moment, which in turn influence the orientation, are introduced. Various ways of ensuring functional immobilization through tuning of both the enzyme and the electrode surface are then described. Finally, the review deals with analytical techniques that have enabled characterization and quantification of successful achievement of the desired orientation. The rich contributions of electrochemistry, spectroscopy (especially infrared spectroscopy), modeling, and microscopy are featured, along with their limitations.

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21

Johnson, D. L., A. J. Conley, and L. L. Martin. "Direct electrochemistry of human, bovine and porcine cytochrome P450c17." Journal of Molecular Endocrinology 36, no. 2 (April 2006): 349–59. http://dx.doi.org/10.1677/jme.1.01971.

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The direct electrochemistry of human, bovine and porcine cytochrome P450c17 (CYP17) has been examined on an edge-oriented pyrolytic graphite electrode. The recombinant protein was immobilized on an electrode modified with a surfactant to simulate the environment of a biological membrane, and hence physiological electron-transfer conditions. The P450 enzymes all retained ‘electron-transfer’ activity while immobilized at the electrode surface as assessed by the presence of catalytic signals under aerobic conditions. The redox potentials for porcine P450c17 were more positive (anodic) than both the human and bovine forms, perhaps reflecting the differences in substrate specificity for these species. In addition, these enzymes were all influenced by pH, consistent with a single proton associated with the single electron-transfer event. Ionic strength of the buffer medium also shifted the redox potentials towards positive, suggesting that electrostatic forces contribute to the protein environment required for the electron-transfer process. The effect of substrate on the redox potential for each P450c17 was measured in the presence of pregnenolone, progesterone, 17α-hydroxypregnenolone and 17α-hydroxyprogesterone. However, no influence on the redox parameters was observed.

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22

Vannoy, Kathryn J., Andrey Ryabykh, Andrei I. Chapoval, and Jeffrey E. Dick. "Single enzyme electroanalysis." Analyst 146, no. 11 (2021): 3413–21. http://dx.doi.org/10.1039/d1an00230a.

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Traditional enzymology relies on the kinetics of millions of enzymes, an experimental approach that may wash out heterogeneities between individual enzymes. Electrochemical methods have emerged in the last 5 years to probe single enzyme reactivity.

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23

KASHIWAGI, Yoshitomo, Qinghai PAN, Yoshinori YANAGISAWA, Norihiko SHIBAYAMA, and Tetsuo OSA. "The Effects of Chain Length of Ferrocene Moiety on Electrical Communication of Mediators-and Enzymes-modified Electrodes." Denki Kagaku oyobi Kogyo Butsuri Kagaku 62, no. 12 (December 5, 1994): 1240–46. http://dx.doi.org/10.5796/electrochemistry.62.1240.

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24

Bernhardt, Paul V. "ChemInform Abstract: Exploiting the Versatility and Selectivity of Mo Enzymes with Electrochemistry." ChemInform 42, no. 21 (April 28, 2011): no. http://dx.doi.org/10.1002/chin.201121252.

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25

E. Ferapontova, Elena, and Lo Gorton. "Direct electrochemistry of heme multicofactor-containing enzymes on alkanethiol-modified gold electrodes." Bioelectrochemistry 66, no. 1-2 (April 2005): 55–63. http://dx.doi.org/10.1016/j.bioelechem.2004.04.004.

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26

Jenner, Leon P., and Julea N. Butt. "Electrochemistry of surface-confined enzymes: Inspiration, insight and opportunity for sustainable biotechnology." Current Opinion in Electrochemistry 8 (March 2018): 81–88. http://dx.doi.org/10.1016/j.coelec.2018.03.021.

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27

Rüdel, Ulrich, Oliver Geschke, and Karl Cammann. "Entrapment of enzymes in electropolymers for biosensors and graphite felt based flow-through enzyme reactors." Electroanalysis 8, no. 12 (December 1996): 1135–39. http://dx.doi.org/10.1002/elan.1140081212.

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28

Flanagan, Lindsey A., and Alison Parkin. "Electrochemical insights into the mechanism of NiFe membrane-bound hydrogenases." Biochemical Society Transactions 44, no. 1 (February 9, 2016): 315–28. http://dx.doi.org/10.1042/bst20150201.

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Hydrogenases are enzymes of great biotechnological relevance because they catalyse the interconversion of H2, water (protons) and electricity using non-precious metal catalytic active sites. Electrochemical studies into the reactivity of NiFe membrane-bound hydrogenases (MBH) have provided a particularly detailed insight into the reactivity and mechanism of this group of enzymes. Significantly, the control centre for enabling O2 tolerance has been revealed as the electron-transfer relay of FeS clusters, rather than the NiFe bimetallic active site. The present review paper will discuss how electrochemistry results have complemented those obtained from structural and spectroscopic studies, to present a complete picture of our current understanding of NiFe MBH.

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29

Bartlett, P. N., and R. G. Whitaker. "Electrochemical immobilisation of enzymes." Journal of Electroanalytical Chemistry and Interfacial Electrochemistry 224, no. 1-2 (June 1987): 27–35. http://dx.doi.org/10.1016/0022-0728(87)85081-7.

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30

Bartlett, P. N., and R. G. Whitaker. "Electrochemical immobilisation of enzymes." Journal of Electroanalytical Chemistry and Interfacial Electrochemistry 224, no. 1-2 (June 1987): 37–48. http://dx.doi.org/10.1016/0022-0728(87)85082-9.

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31

Melanori, B. A. "Covalent Catalysis by Enzymes." Bioelectrochemistry and Bioenergetics 15, no. 1 (February 1986): 142. http://dx.doi.org/10.1016/0302-4598(86)80018-6.

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32

SUN, Dongmei. "Immobilization and direct electrochemistry of cop-per-containing enzymes on ac-tive carbon." Chinese Science Bulletin 49, no. 23 (2004): 2452. http://dx.doi.org/10.1360/04wb0070.

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33

Yang, Chi, Chunxiang Xu, and Xuemei Wang. "ZnO/Cu Nanocomposite: A Platform for Direct Electrochemistry of Enzymes and Biosensing Applications." Langmuir 28, no. 9 (February 22, 2012): 4580–85. http://dx.doi.org/10.1021/la2044202.

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34

de Poulpiquet, A., A. Ciaccafava, R. Gadiou, S. Gounel, M. T. Giudici-Orticoni, N. Mano, and E. Lojou. "Design of a H2/O2 biofuel cell based on thermostable enzymes." Electrochemistry Communications 42 (May 2014): 72–74. http://dx.doi.org/10.1016/j.elecom.2014.02.012.

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35

McMillan, Duncan G. G., Sophie J. Marritt, Gemma L. Kemp, Piers Gordon-Brown, Julea N. Butt, and Lars J. C. Jeuken. "The impact of enzyme orientation and electrode topology on the catalytic activity of adsorbed redox enzymes." Electrochimica Acta 110 (November 2013): 79–85. http://dx.doi.org/10.1016/j.electacta.2013.01.153.

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36

SUGIMOTO, Yu, Yuki KITAZUMI, Osamu SHIRAI, and Kenji KANO. "Effects of Mesoporous Structures on Direct Electron Transfer-Type Bioelectrocatalysis: Facts and Simulation on a Three-Dimensional Model of Random Orientation of Enzymes." Electrochemistry 85, no. 2 (2017): 82–87. http://dx.doi.org/10.5796/electrochemistry.85.82.

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37

Han, Lianhuan, Wei Wang, Jacques Nsabimana, Jia-Wei Yan, Bin Ren, and Dongping Zhan. "Single molecular catalysis of a redox enzyme on nanoelectrodes." Faraday Discussions 193 (2016): 133–39. http://dx.doi.org/10.1039/c6fd00061d.

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Due to a high turnover coefficient, redox enzymes can serve as current amplifiers which make it possible to explore their catalytic mechanism by electrochemistry at the level of single molecules. On modified nanoelectrodes, the voltammetric behavior of a horseradish peroxidase (HRP) catalyzed hydroperoxide reduction no longer presents a continuous current response, but a staircase current response. Furthermore, single catalytic incidents were captured through a collision mode at a constant potential, from which the turnover number of HRP can be figured out statistically. In addition, the catalytic behavior is dynamic which may be caused by the orientation status of HRP on the surface of the electrode. This modified nanoelectrode methodology provides an electrochemical approach to investigate the single-molecule catalysis of redox enzymes.

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38

Yehezkeli, Omer, Oded Ovits, Ran Tel-Vered, Sara Raichlin, and Itamar Willner. "Reconstituted Enzymes on Electropolymerizable FAD-Modified Metallic Nanoparticles: Functional Units for the Assembly of Effectively “Wired” Enzyme Electrodes." Electroanalysis 22, no. 16 (August 2010): 1817–23. http://dx.doi.org/10.1002/elan.201000197.

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39

Rapson, Trevor D., Ulrike Kappler, and Paul V. Bernhardt. "Direct catalytic electrochemistry of sulfite dehydrogenase: Mechanistic insights and contrasts with related Mo enzymes." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1777, no. 10 (October 2008): 1319–25. http://dx.doi.org/10.1016/j.bbabio.2008.06.005.

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40

Zebda, A., L. Renaud, M. Cretin, F. Pichot, C. Innocent, R. Ferrigno, and S. Tingry. "A microfluidic glucose biofuel cell to generate micropower from enzymes at ambient temperature." Electrochemistry Communications 11, no. 3 (March 2009): 592–95. http://dx.doi.org/10.1016/j.elecom.2008.12.036.

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41

Liu, Jinping, Chunxian Guo, Chang Ming Li, Yuanyuan Li, Qingbo Chi, Xintang Huang, Lei Liao, and Ting Yu. "Carbon-decorated ZnO nanowire array: A novel platform for direct electrochemistry of enzymes and biosensing applications." Electrochemistry Communications 11, no. 1 (January 2009): 202–5. http://dx.doi.org/10.1016/j.elecom.2008.11.009.

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42

Gorton, L. "Carbon paste electrodes modified with enzymes, tissues, and cells." Electroanalysis 7, no. 1 (January 1995): 23–45. http://dx.doi.org/10.1002/elan.1140070104.

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43

Lobo, Maria Jesús, Arturo J. Miranda, and Paulino Tuñón. "Amperometric biosensors based on NAD(P)-dependent dehydrogenase enzymes." Electroanalysis 9, no. 3 (February 1997): 191–202. http://dx.doi.org/10.1002/elan.1140090302.

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44

Lohmann, Wiebke, and Uwe Karst. "Electrochemistry meets enzymes: instrumental on-line simulation of oxidative and conjugative metabolism reactions of toremifene." Analytical and Bioanalytical Chemistry 394, no. 5 (January 13, 2009): 1341–48. http://dx.doi.org/10.1007/s00216-008-2586-7.

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45

Sandeep, S., A. S. Santhosh, N. K. Swamy, G. S. Suresh, and J. S. Melo. "Detection of Catechol Using a Biosensor Based on Biosynthesized Silver Nanoparticles and Polyphenol Oxidase Enzymes." Portugaliae Electrochimica Acta 37, no. 4 (2019): 257–70. http://dx.doi.org/10.4152/pea.201904257.

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46

Stoytcheva, Margarita, Roumen Zlatev, Zdravka Velkova, Velizar Gochev, Alan Ayala, Gisela Montero, and Benjamín Valdez. "Diazirine‐functionalized Nanostructured Platform for Enzymes Photografting and Electrochemical Biosensing." Electroanalysis 31, no. 8 (May 22, 2019): 1526–34. http://dx.doi.org/10.1002/elan.201900086.

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47

Brown, D. E. "Enzymes in Industry — Production and Applications." Biosensors and Bioelectronics 6, no. 8 (January 1991): 709. http://dx.doi.org/10.1016/0956-5663(91)87026-8.

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48

Mottola, Horacio A. "Enzymes as analytical reagents: substrate determinations with soluble and with immobilised enzyme preparations. Plenary lecture." Analyst 112, no. 6 (1987): 719. http://dx.doi.org/10.1039/an9871200719.

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49

IMABAYASHI, Shin-ichiro, Miki KASHIWA, and Masayoshi WATANABE. "Immobilization of Horseradish Peroxidase on Binary Self-assembled Monolayers with Carboxyl- and Hydroxyl-terminal Groups: Dependence of the Amount of Immobilized Enzymes and Their Electrocatalytic Activity on the Monolayer Composition." Electrochemistry 74, no. 2 (2006): 186–88. http://dx.doi.org/10.5796/electrochemistry.74.186.

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50

Esposti, M. Degli. "Enzymes, Receptors and Carriers of Biological Membranes." Bioelectrochemistry and Bioenergetics 15, no. 1 (February 1986): 141–42. http://dx.doi.org/10.1016/0302-4598(86)80017-4.

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