AC Fields 339, 346, 351 Adsorption – Enzymes 14, 250 – Nonspecific 45

Total Page:16

File Type:pdf, Size:1020Kb

AC Fields 339, 346, 351 Adsorption – Enzymes 14, 250 – Nonspecific 45 389 Index a biocathodes 243ff. AC fi elds 339, 346, 351 – air diffusion 252 adsorption – hydrogel-based 252 – enzymes 14, 250 – oxygen reduction reaction (ORR) 243ff. – nonspecifi c 45, 217 – polarization plots 251 – proteins 13f., 174 biocompatible 12, 16, 42ff. – reactivity 111 bioelectrocatalysis, see biocatalysis – surface-specifi c 111 biofuel cell (BFC) 3, 229ff. – vesicle 197f. – development 6, 26 alcohol dehydrogenase 260f. – electron transfer (ET) 29ff. alkanethiols 98, 100 – enzymatic glucose/O2 38 amperometric biosensors 1ff. – enzyme-based, see enzymatic fuel cell anesthesia 377f., 380 (EFC) antibodies 3, 53f. – principle 31 antigen 3, 53f. biofuel cell 2f., 5f., 9f., 29, 31f., 36ff., 55, ascorbate oxidase 244 57 assembled biofuel cells 255 bioinorganic hybrids 85 atomic force microscopy (AFM) 85, 92 biological recognition element 1ff., 7, 16, – contact mode 287 23f., 29, 36, 38, 44ff., 56f., 59 – fl uidity of biomimetic membranes 200f. biological recognition 4, 11 – small unilamellar vesicles 198 – element 27, 45 – TERS 291 biomimetic layers 107f., 143f., 183, 190 atomic force microscopy 85 – fl uidity 200f. Au atom mining 104 – formation of lipid fi lms 194ff. Au–nanoparticle hybrids 120 – gold-supported 201 AuNP–azurin hybrid 123 – rapid solvent exchange 200 AuNP–protein hybrids 123 – vesicle fusion 196ff. azurin 113f., 123, 125 biomimetic membrane 189ff., 200f., 220 biosensor architecture 2f., 5, 13ff., 18ff., b 38f., 55f., 59 bending rigidity 338, 347 biosensor stability 28, 43 between laboratory precision, see – long-term 4, 6, 16, 28, 44 reproducibility – storage 28 bias voltage 92, 95, 97 – working 28 bilayer lipid membranes 107 biosensor bilayer lipid membranes, see membranes – accuracy 28 bilirubin oxidase 244, 246 – amperometric 1ff. bioanodes 235ff. – applications 22 biocatalysis 5f., 122, 232f., 246 – architecture 11, 14ff. Advances in Electrochemical Science and Engineering. Edited by Richard C. Alkire, Dieter M. Kolb, and Jacek Lipkowski © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim ISBN: 978-3-527-32885-7 390 Index – BFC, see biofuel cell cholesterol 107, 175f., 180, 183, 345, 347ff., – characteristics 21, 25 352, 355, 358 – development 8ff. clinical use 369, 377 – dynamic range 27 cofactor 7, 14, 30 – EFC, see enzymatic fuel cell – fl avin adenine dinucleotide (FAD) 32f., – electrochemical 40 42, 232, 235 – fi rst-generation 7, 11 – NAD+ 242, 312f. – glucose 21, 32f., 46, 239 – protein-integrated 30f. – implanted 42ff. coherent multi-electron transfer 105, 126 – nano- 38f., 41 coherent scattering 148, 157, 161f., 171 – nucleic acid-based 48ff. Cole–Cole plot 193ff. – MFC, see microbial fuel cell composite, see hybrid – micro- 44 condensed matter molecular charge transfer – optimization 20, 26 theory 87 – performance 18f., 25ff. conductive polymers 17 – precision, see measurement conductivity – research 23ff. – long-range off-resonance 125 – response 18, 20 – oligonucleotides 99 – second-generation 7f. – short oligonucleotides 97 – set-up 3ff. – single molecules 85f., 98f. – tapered voltammetric enzyme 44 confocal microscopy 336, 343, 348, 355 – third-generation 13f., 232 contrast variation 168, 174 – tip 45 cooperative charge transport 117 – working potential 15 Coulomb charging effects 121 – working range 27 critical poration potential 349f. biosensors 1ff., 5ff., 7ff., 13f., 16ff., 20ff., current 24f., 29f., 32, 36ff., 54ff., 59 – –bias voltage relation 92, 97 Boltzmann constant 88, 338 – density 38, 41, 90, 235, 239f., 250f. Born approximation 151f., 152, 154 – stationary diffusion 41 – distorted wave (DWBA) 154 current–bias relation 95 brain tumor electroporation 381 current–bias voltage relation 97 butanethiol 101 current–overpotential relation 95, 97 cysteine 97, 100, 102f. c cystine 102 cancer 378, 380f., 383ff. cytochrome b562 113, 115, 125 carbon nanotubes (CNT) 235, 242, 250 cytochrome c oxidase (COX) 207 – -modifi ed surface 33 cytochrome c oxidase 116, 123 – multiwalled (MWCNTs) 35, 40, 250f., cytochrome c 113 260 cytochrome c4 116, 118 – nanobiosensors 39ff. – single-walled (SWCNTs) 40, 242, 251 d catalytic enzyme activity 5, 15, 32 DC pulses 339ff. cell homeostasis 373 de Broglie waves 144 cellobiose dehydrogenase 242 Debye length 41 cells 369f., 372ff., 376f., 379, 382ff. density functional theory (DFT) 102f., channel 294f. – -forming lipid 210 deposition – ion- 216f., 219 – electro- 289 – micro- 256 – Langmuir–Blodgett 285 – single 213f. – pinhole free 279 charge diffusion 16f., 19, 25, 35f., 39, 41, 45, 55, – repulsion 20 58, 60 – transport mechanism 98 – analyte 45 charged lipids 345, 349f., 358 – coeffi cient of lipids 337 Index 391 – -controlled electrode process 35, 46 – working 93, 161f., 257 – lateral 202 electrodeformation 338ff. – linear 41 electrodeposition polymers 58 – oxygen 250 electrodeposition 10, 17, 20, 37, 40, 58 1,2-dimyristoyl-sn-glycero-3-phosphocholine – metal nanoparticles 40 107 – paints (EDPs) 37f., 42 dimyristoylphosphatidylcholine (DMPC) electron transfer (ET) 3, 6, 337, 350, 107f., 168f., 180f., 183, 202f. 353ff. Dirac delta function 153 – biofuel cells 29ff. direct electron transfer 2, 9, 232f. – biosensors 29ff. direct inversion 184 – cascades 14ff. DNA conduction 98 – coherent multi- 105, 126 DNA monolayers 173f. – direct (DET) 13f., 29, 232ff. DNA-based molecules 98 – distances 18, 33, 35 DPTL 191, 193, 201, 205ff., 210 – electrochemical 88ff. drug delivery 369ff. – heterogeneous 197, 310 – interfacial 87f., 98, 105, 112 e – intramolecular 112, 118, 244 edge tension 338, 341, 344, 348, 350ff. – long-range interfacial 90f. electric tension 339 – mediated (MET) 15, 36f., 233ff. electrochemical impedance spectroscopy – molecular 86 (EIS) 54f., 92, 191ff. – pathway 7, 16, 29, 32 – Cole–Cole plot 195 – rate-limiting effect 36 – lipid bilayers 191ff. – rates 6, 36f. – Nyquist plot 212f. – reversible 14 – spacer-based tBLMs 204f. – self-exchange collisions 241 – thiolipid-based tBLMs 205ff. – single steps 95 electrochemical – two- 35, 118 – cell confi guration 161ff. electron transfer 2f., 9, 57, 59 – double layer 96 electron tunneling 13, 87ff. electrochemotherapy 371, 377ff., 386 – coherent multi- 87 electrode surface – diabatic 91 – functionalized 29, 32 – factor 89f. – modifi cation 15 – single-molecule 94 – passivation 45 electron tunneling factor 89f. – redox proteins 29 electron electrode 371f., 375ff., 381f. – acceptors 15, 87, 91, 233 – carbon-fi ber micro- 44 – donors 15, 87 – carbon paper 252 – exchange energy 88 – CNT-modifi ed 40f. – hopping 36, 98, 125 – counter 93, 209, 257 electronic spillover 123 – glassy carbon 35, 41, 239, 249, 257 electronic transmission coeffi cient 88, – graphite felt 250 96 – fouling 20, 40, 44 electronic – gold 41, 46, 107f. – broadening 95 – interdigitated (IDE) 54 – transmission coeffi cient 88, 96 – macro- 42 electropermeabilization 370, 371f., 376 – mercury 14 electrophoretic 370, 375f. – micro- 41, 44f., 47 electroporation 369ff. – nano- 39, 41 electroporation threshold 341, 349 – nanogap 88, 92, 94 electroporation, see membrane – reference 93, 161f., 214 electroporation – single-crystal 100 electrorefl ectance spectroscopy 92 – three-dimensional 259f. electrotransfer 369ff. 392 Index endoscopic electroporation 377 gene electrotransfer 369ff. enzymatic fuel cell (EFC) 31, 229ff. giant unilamellar vesicle (GUV) 337ff., – design 231, 233 344, 348, 350f., 353, 356 – enzyme electron transfer 231ff. glucose dehydrogenases 32ff. – glucose–oxygen 256, 257f. glucose oxidase (GOx) 1f., 7, 9, 21, 32, 34, – long-term stability 230 57, 235ff. – membraneless 230, 242 glucose oxidation 235, 240ff., 255 – microfl uidic 256 gold contrast-matched water 165 – modular stack half-cell 257 gold nanoparticles 112, 120 – redox polymer-mediated 258f. gold-supported thiolipid-based tBLM 205, – –sensor system 230 210 – thermodynamic losses 239 gramicidin 107f., 194, 203f., 207ff., 216 enzyme cascade 243, 259, 261 Green function 91 enzyme electrodes 59 enzyme 3, 5f., 9f., 14ff., 18, 29, 31f., 42, 44, h 46, 48f., 57f., 60 Heaviside function 153 – activity 5f., 15, 17, 20, 32 4α-helix proteins 113f. – apo- 231f. heme group proteins 113 – co- 231f. high-throughput screening 41 – cofactor 7, 14, 30, 232 homocysteine 97, 100 – covalent attachment 14, 29 horse heart cytochrome c 114 – dehydrogenases 30, 32 human insulin 106, 109, 111 – electrodes 3 hybrid bilayers 170, 173 – inhibitors 6 hybrid – laccase 29 – Au–nanoparticle 120ff. – metallo- 112, 114 – DMPC–cholesterol vesicles 180f., 183, – multiple copper oxidases (MCOs) 244ff. 203 – peroxidases 29, 32 – enzyme–nanoparticle 35, 42, 94 – stability 6, 12 – lipid–DNA 174 – wild-type 114f., 241f. – metalloprotein–nanoparticle 113 extracellular volume 373f., 376 – polymer–lipid 217 – SLN–ATP 212f. f hybridization fast digital imaging 339, 351, 358 – detection 50ff. Fermi pseudo potential 147 – plasmon 281 Fermi – probe–target 52 – energy 88, 94 – surface hybridization assays 51 – level 93ff. hydrogenase 235, 242 – potential 149 hydrogen-bonded networks 97 – pseudo potential 147 hydrophilic spacer 190ff., 196, 201, 204, ferrocene 239f. 206, 211, 215f., 222 Fick’s fi rst law 197 hydrophilic “fi rst-generation” biosensors 7, 11 – amino acids 112 fl avin adenine dinucleotide 232 – domain 190 fl uorescence recovery after photobleaching – redox hydrogels 36 (FRAP) 200 – spacers 190f., 207 – thiolipid-based tBLMs 215 hydrophobic – spacer-based tBLMs 204 – binders 250 fructose dehydrogenase 242 – domain 190 fusion dynamics 354 – surfaces 101, 174, 191, 197 g i gated intramolecular electron transfer 118 imaging gel-phase
Recommended publications
  • Electro-Organic Reactions and Redox Active Biomolecules: a Student Diary*
    these techniques. Some group members also told me that they use liquid chromatography-mass spectrometry (LC- MS), and it is a great help in analyzing their reaction products. Methods like atomic force microscopy, scanning electron microscopy, and surface FTIR are used in the group for characterization of the electrode surfaces they make. A week or so later: I have done my first electrochemical synthesis experiment. I did cyclic voltammetry Electro-organic Reactions in undergraduate analytical lab, so it was not totally new. The reactor cell I used was like two connected beakers in a water jacket (Fig. 1). One beaker is and Redox Active Biomolecules: the working electrode compartment, and the other is the counter electrode compartment, separated by a salt bridge. A Student Diary* This is so that products from the two compartments do not combine to give by James F. Rusling and Albert J. Fry undesirable products. The reactor had a carbon cloth working electrode, which is a cool material, like a conducting It is early December, and I have been in chemistry grad school black fabric that you cut to the right for about 3 months. It is a big transition, and a bit tougher size with scissors. It has a large surface than I expected. The courses are not too hard, but the focus area to facilitate the catalytic reaction. The reactor has counter and reference here is very much on research. I have chosen the group in electrodes, and is hooked up to a which I will do my thesis research, and I am happy about that.
    [Show full text]
  • Application of Voltammetry in Biomedicine-Recent
    Macedonian Journal of Chemistry and Chemical Engineering, Vol. 39, No. 2, pp. 153–166 (2020) MJCCA9 – 803 ISSN 1857-5552 e-ISSN 1857-5625 Received: September 23, 2020 DOI: 10.20450/mjcce.2020.2152 Accepted: October 8, 2020 Original scientific paper APPLICATION OF VOLTAMMETRY IN BIOMEDICINE RECENT ACHIEVEMENTS IN ENZYMATIC VOLTAMMETRY Rubin Gulaboski1, Valentin Mirceski2,3 1Faculty of Medical Sciences, Goce Delčev University, Štip, Republic of Macedonia 2Faculty of Natural Sciences and Mathematics, Ss. Cyril and Methodius University, Skopje, Republic of Macedonia 3Department of Inorganic and Analytical Chemistry, University of Lodz, Tamka 12, 91-403 Lodź, Poland [email protected]; [email protected] Protein-film voltammetry (PFV) is considered the simplest methodology to study the electrochem- istry 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 meta- bolic 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.
    [Show full text]
  • Electrochemical Evidence That Pyranopterin Redox Chemistry Controls the Catalysis of Yedy, a Mononuclear Mo Enzyme
    Electrochemical evidence that pyranopterin redox chemistry controls the catalysis of YedY, a mononuclear Mo enzyme Hope Adamsona, Alexandr N. Simonovb, Michelina Kierzekc, Richard A. Rotheryc, Joel H. Weinerc, Alan M. Bondb, and Alison Parkina,1 aDepartment of Chemistry, University of York, Heslington, York YO10 5DD, United Kingdom; bSchool of Chemistry, Monash University, Clayton, VIC 3800, Australia; and cDepartment of Biochemistry, University of Alberta, Edmonton, AB T6G 2H7, Canada Edited by Harry B. Gray, California Institute of Technology, Pasadena, CA, and approved October 13, 2015 (received for review August 25, 2015) A long-standing contradiction in the field of mononuclear Mo explores the possibility that ligand-based redox chemistry plays a enzyme research is that small-molecule chemistry on active-site mimic role in YedY catalysis. compounds predicts ligand participation in the electron transfer YedY has been structurally characterized via both X-ray crys- reactions, but biochemical measurements only suggest metal-cen- tallography and X-ray absorption spectroscopy (XAS) (3, 8, 9). In tered catalytic electron transfer. With the simultaneous measurement most mononuclear Mo enzymes, heme groups and iron sulfur of substrate turnover and reversible electron transfer that is provided clusters are found within the same protein as the Mo center, but the by Fourier-transformed alternating-current voltammetry, we show only metal site in YedY is Mo, making this enzyme a helpfully that Escherichia coli YedY is a mononuclear Mo enzyme that recon- simple system for studying redox chemistry (Fig. 1) (1, 3). Within ciles this conflict. In YedY, addition of three protons and three elec- the active site, the X-ray structure was interpreted to show Mo(V) trons to the well-characterized “as-isolated” Mo(V) oxidation state is in a square pyramidal environment (3), identical to other members needed to initiate the catalytic reduction of either dimethyl sulfoxide of the “sulfite oxidase” family of mononuclear Mo enzymes.
    [Show full text]
  • Electrochemical Properties of Gsnos by Protein Film Voltammetry
    180 Chapter 6 Electrochemical Properties of gsNOS by Protein Film Voltammetry 181 6.1 Abstract The accurate measurement of a protein’s electrochemical properties is an important part of understanding its function. Several methods have been developed to facilitate communication between deeply buried protein metal centers and electrodes. One such technique, protein film voltammetry (PFV), involves the immobilization of proteins on the surface of electrodes by various means. Such techniques can result in clear signals from proteins, allowing the measurement of not only reduction potentials but kinetics as well. Two types of PFV have been employed in the study of the nitric oxide sythase from Geobacillus stearothermophilus. First, a mutant of this NOS was covalently connected to a gold electrode. It was hypothesized that the use of a hydrophilic linker would maintain a normal aqueous environment around the enzyme and avoid the shifting of potentials (a common problem in PFV). When it was found that this technique still resulted in measuring responses with significantly shifted potentials (as compared with those measured by redox titration in solution), a more traditional film was employed. The kinetics of gsNOS was studied in DDAB films and compared with the mammalian inducible isoform. It was found to show similar behavior, and experiments are still underway to further characterize the kinetics of wild type and three mutants of gsNOS (W70H, W70F, and W70Y, introduced in Chapter 3). 182 6.2 Introduction and Background Key to the function of most metalloenzymes is the redox activity of transition metals. These metals have the unique ability, as distinct from most organic molecules, to easily access multiple oxidation states.
    [Show full text]
  • Direct Electrochemistry of Redox Enzymes As a Tool for Mechanistic Studies Christophe Léger, Patrick Bertrand
    Direct Electrochemistry of Redox Enzymes as a Tool for Mechanistic Studies Christophe Léger, Patrick Bertrand To cite this version: Christophe Léger, Patrick Bertrand. Direct Electrochemistry of Redox Enzymes as a Tool for Mech- anistic Studies. Chemical Reviews, American Chemical Society, 2007, 108, 10.1021/cr0680742. hal- 01211439 HAL Id: hal-01211439 https://hal.archives-ouvertes.fr/hal-01211439 Submitted on 5 Oct 2015 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. Chem. Rev. 2008, 108, 2379–2438 2379 Direct Electrochemistry of Redox Enzymes as a Tool for Mechanistic Studies Christophe Le´ger* and Patrick Bertrand Laboratoire de Bioe´nerge´tique et Inge´nierie des Prote´ines, CNRS UPR 9036, IBSM, and Universite´ de Provence, 31 chemin Joseph Aiguier, 13402 Marseille Cedex 20, France Received August 1, 2007 Contents 5. List of Abbreviations 2432 6. Acknowledgments 2432 1. Introduction 2379 7. Supporting Information Available 2432 2. Modeling the Voltammetry of Adsorbed Redox 2382 8. References 2432 Enzymes 2.1. Noncatalytic Voltammetry 2382 1. Introduction 2.1.1. The Case of Pure Electron Transfer (ET) 2382 2.1.2. Chemical Processes Coupled to ET 2387 This review regards the use of dynamic electrochemistry 2.2.
    [Show full text]
  • Probing Biological Redox Chemistry with Large Amplitude Fourier Transformed Ac Voltammetry Chemcomm
    Volume 53 Number 69 7 September 2017 Pages 9507–9650 ChemComm Chemical Communications rsc.li/chemcomm ISSN 1359-7345 FEATURE ARTICLE Alan M. Bond, Alison Parkin et al. Probing biological redox chemistry with large amplitude Fourier transformed ac voltammetry ChemComm View Article Online FEATURE ARTICLE View Journal | View Issue Probing biological redox chemistry with large amplitude Fourier transformed ac voltammetry Cite this: Chem. Commun., 2017, 53, 9519 Hope Adamson,a Alan M. Bond*b and Alison Parkin *a Biological electron-exchange reactions are fundamental to life on earth. Redox reactions underpin Received 18th May 2017, respiration, photosynthesis, molecular biosynthesis, cell signalling and protein folding. Chemical, Accepted 12th June 2017 biomedical and future energy technology developments are also inspired by these natural electron transfer DOI: 10.1039/c7cc03870d processes. Further developments in techniques and data analysis are required to gain a deeper understanding of the redox biochemistry processes that power Nature. This review outlines the new insights gained from rsc.li/chemcomm developing Fourier transformed ac voltammetry as a tool for protein film electrochemistry. Creative Commons Attribution 3.0 Unported Licence. Introduction Biological redox reactions are mediated by both small and large molecules, ranging from species such as quinones, which resemble typical synthetic chemistry redox reagents, to complex metalloenzymes comprising ‘‘wires’’ of redox-active centers (i.e. cytochrome c oxidase, the enzyme responsible for converting O2 1 to H2O in the mitochondria of all human cells, see Fig. 1). Redox reactions even underpin some DNA repair mechanisms.2,3 This This article is licensed under a review focuses on redox active proteins and enzymes, and the new mechanistic insights which can be gained by integrating the technique of large amplitude Fourier transformed voltammetry4 (FTacV) into the toolbox of protein film electrochemistry.
    [Show full text]
  • Relation Between Anaerobic Inactivation and Oxygen Tolerance in a Large Series of Nife Hydrogenase Mutants
    Relation between anaerobic inactivation and oxygen tolerance in a large series of NiFe hydrogenase mutants Abbas Abou Hamdana, Pierre-Pol Liebgottb, Vincent Fourmonda, Oscar Gutiérrez-Sanzc, Antonio L. De Laceyc, Pascale Infossia, Marc Rousseta, Sébastien Dementina, and Christophe Légera,1 aLaboratoire de Bioénergétique et Ingénierie des Protéines, Centre National de la Recherche Scientifique, Aix-Marseille Université, Institut de Microbiologie de la Méditerranée, 13402 Marseille Cedex 20, France; bLaboratoire de Microbiologie, Institut de Recherche pour le Développement, Aix Marseille Université, Unité Mixte de Recherche D180, Microbiologie et Biotechnologie des Environnements Chauds, Ecole Supérieure d’Ingénieurs de Luminy, 13288 Marseille Cedex 09, France; and cLaboratorio de Bioelectrocatalisis, Departamento de Biocatalisis, Instituto de Catalisis y Petroleoquimica, Consejo Superior de Investigaciones Cientificas, 28049 Madrid, Spain Edited* by Jean-Michel Savéant, Université Paris Diderot (Paris 7), Paris, France, and approved October 19, 2012 (received for review July 29, 2012) Nickel-containing hydrogenases, the biological catalysts of H2 investigations have shown that in O2-resistant enzymes, it is an oxidation and production, reversibly inactivate under anaerobic, unprecedented 4Fe3S cluster (8–10) that has a high reduction oxidizing conditions. We aim at understanding the mechanism of potential and the ability to cycle through three redox states in (in)activation and what determines its kinetics, because there is a narrow range of potential (11). a correlation between fast reductive reactivation and oxygen tol- The rate of reactivation of NiB partly determines O2 toler- erance, a property of some hydrogenases that is very desirable ance, but the reason this reaction is orders of magnitude faster in oxygen-resistant hydrogenases than in standard hydrogenases from the point of view of biotechnology.
    [Show full text]
  • Membrane Protein Modified Electrodes in Bioelectrocatalysis
    catalysts Review Membrane Protein Modified Electrodes in Bioelectrocatalysis Huijie Zhang y, Rosa Catania y and Lars J. C. Jeuken * School of Biomedical Sciences and the Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 9JT, UK; [email protected] (H.Z.); [email protected] (R.C.) * Correspondence: [email protected]; Tel.: +44-113-343-3829 These authors have contributed equally. y Received: 18 November 2020; Accepted: 3 December 2020; Published: 6 December 2020 Abstract: Transmembrane proteins involved in metabolic redox reactions and photosynthesis catalyse a plethora of key energy-conversion processes and are thus of great interest for bioelectrocatalysis- based applications. The development of membrane protein modified electrodes has made it possible to efficiently exchange electrons between proteins and electrodes, allowing mechanistic studies and potentially applications in biofuels generation and energy conversion. Here, we summarise the most common electrode modification and their characterisation techniques for membrane proteins involved in biofuels conversion and semi-artificial photosynthesis. We discuss the challenges of applications of membrane protein modified electrodes for bioelectrocatalysis and comment on emerging methods and future directions, including recent advances in membrane protein reconstitution strategies and the development of microbial electrosynthesis and whole-cell semi-artificial photosynthesis. Keywords: membrane protein; bioelectrocatalysis; electrode modification; biofuel cells; photosynthesis; liposomes; hybrid vesicles; microbial electrosynthesis 1. Introduction Membrane proteins constitute 20–30% of all proteins encoded by both prokaryotic and eukaryotic cells. They perform a wide variety of functions, including material transport, signal transduction, catalysis, proton and electron transport (Figure1)[ 1]. They are also key to a number of earth’s most fundamental reactions, such as respiration and photosynthesis [2,3].
    [Show full text]
  • Protein Film Voltammetry
    View Article Online / Journal Homepage / Table of Contents for this issue Reactions of complex metalloproteins studied by protein-film voltammetry Fraser A. Armstrong, Hendrik A. Heering and Judy Hirst Inorganic Chemistry Laboratory, Oxford University, Oxford, UK OX1 3QR The following review explores applications of voltammetric systems. The approach we will describe stems from the original methods for observing reactions of complex metalloproteins. discoveries of Hill and of Kuwana and their coworkers1.2who Attention is focused upon the technique of ‘protein-film first demonstrated reversible, diffusion-controlled voltammetry voltammetry’, in which the protein molecules under in- of cytochrome c at a solid electrode without mediators and with vestigation are adsorbed on the electrode surface and no sign of denaturation. The all-important feature is application electrochemically ‘interrogated.’The experiments address a of a controlled electrochemical potential which is varied either minuscule sample with high sensitivity, and optimal control continuously or in steps or pulses: this activates specific redox over both potential and time dependence of reactions. centres, the reactions of which are measured simultaneously Factors governing the voltammetric response are outlined, through the current response, thereby procuring interdependent and particular emphasis is given to the ability to study thermodynamic and kinetic information from a single set of reactions that are coupled to and may ‘gate’ the primary experiments. The interactive nature of the experiments is electron exchange processes. Examples described include optimised by confining the sample under investigation to the proton-transfer and metal-binding reactions of iron-sulfur electrode surface, in a configuration which we refer to as clusters, coupling of electron transfer in peroxidases, quanti- ‘protein-film voltammetry’ and upon which we will focus our fying electron-transport pathways in multi-centred enzy- discussion.
    [Show full text]
  • A New Electrochemical Cell with a Uniformly Accessible Electrode To
    A new electrochemical cell with a uniformly accessible electrode to study fast catalytic reactions Mariam Fadel, Daurelle Jean-Vincent, Vincent Fourmond, Jérôme Vicente To cite this version: Mariam Fadel, Daurelle Jean-Vincent, Vincent Fourmond, Jérôme Vicente. A new electrochemical cell with a uniformly accessible electrode to study fast catalytic reactions. Physical Chemistry Chemical Physics, Royal Society of Chemistry, 2019, 21 (23), pp.12360-12371. 10.1039/c9cp01487j. hal- 02308533 HAL Id: hal-02308533 https://hal.archives-ouvertes.fr/hal-02308533 Submitted on 29 Jan 2020 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. A New Electrochemical Cell with uniformly Accessible Electrode to Study Fast Catalytic Reactions Mariam Fadel*1,2, Jean-Vincent Daurelle*1, Vincent Fourmond2, Jérôme Vicente1 1Laboratoire IUSTI (UMR AMU-CNRS 7343) Polytech Marseille, Dpt Mécanique Energétique (ME) Technopôle de Chateau Gombert 5 rue Enrico Fermi 13453 Marseille cedex 13 2Aix-Marseille Université, CNRS, BIP UMR 7281, 31 chemin J. Aiguier, F-13402 Marseille cedex 20, France *Email : [email protected] , [email protected] Abstract Electrochemical study of fast catalytic reactions is limited by mass transport using the conventional electrochemical cell of Rotating disk electrode (RDE) [4].
    [Show full text]
  • Chapter 2: the Ph-Dependent Redox Inactivation of Amicyanin As Studied by Rapid Protein- Film Voltammetry
    Chapter 2 Chapter 2: The pH-dependent redox inactivation of amicyanin as studied by rapid protein- film voltammetry Abstract The redox properties of the blue copper protein amicyanin have been studied with slow and rapid scan protein-film cyclic voltammetry. At slow scan rates, when the system is able to equilibrate with the electrode potential, the reduction potential of amicyanin depends on pH in a sigmoidal manner. The data are analysed by assuming that a single titrating group with a redox state dependent pKa is responsible for the pH-dependence of red ox the reduction potential, which gave pKa = 6.3, pKa £ 3.2 at 22 °C. Voltammetry at higher scan rates shows that the low-pH form of amicyanin is not oxidised directly. Instead, oxidation occurs only after conversion to the high-pH form. Simulations show that this conversion is achieved with a rate constant > 750 s-1 at 25 °C. In order to slow the coupled reaction down, the experiments were performed at 0 °C, at which a rate constant of 35 ± 20 s-1 was determined. In conjunction with evidence from NMR, the data are discussed within a scheme that incorporates protonation and dissociation of the copper coordinating histidine 96 in the reduced form. 27 Protein film voltammetry on amicyanin Introduction This paper deals with the dynamics of the pH-dependent conformational change that occurs in the active site of the small blue copper protein, amicyanin. Amicyanin functions as the obligatory electron acceptor of methylamine dehydrogenase (MADH) [Husain et al., 1985; Tobari et al., 1981; van Houwelingen et al., 1985; van Spanning et al., 1990], an enzyme that is essential when bacteria like Paracoccus versutus are grown on mimimal medium with methylamine as the sole source of carbon, nitrogen and energy [Dennison et al., 1998].
    [Show full text]
  • Short Circuiting a Sulfite Oxidising Enzyme with Direct Electrochemistry
    Biochimica et Biophysica Acta 1807 (2011) 108–118 Contents lists available at ScienceDirect Biochimica et Biophysica Acta journal homepage: www.elsevier.com/locate/bbabio Short circuiting a sulfite oxidising enzyme with direct electrochemistry: Active site substitutions and their effect on catalysis and electron transfer Trevor D. Rapson a, Ulrike Kappler a, Graeme R. Hanson b, Paul V. Bernhardt a,⁎ a Centre for Metals in Biology, School of Chemistry and Molecular Biosciences, University of Queensland, Brisbane, 4072, Australia b Centre for Advanced Imaging, University of Queensland, Brisbane, 4072, Australia article info abstract Article history: Sulfite dehydrogenase (SDH) from Starkeya novella is a heterodimeric enzyme comprising a Mo active site and Received 14 July 2010 a heme c electron relay, which mediates electron transfer from the Mo cofactor to cytochrome c following Received in revised form 6 September 2010 sulfite oxidation. Studies on the wild type enzyme (SDHWT) and its variants have identified key amino acids at Accepted 15 September 2010 the active site, specifically Arg-55 and His-57. We report the MoVI/V,MoV/IV and FeIII/II (heme) redox potentials Available online 20 September 2010 of the variants SDHR55K, SDHR55M, SDHR55Q and SDHH57A in comparison with those of SDHWT. For SDHR55M, SDHR55Q and SDHH57A the heme potentials are lowered from ca. 240 mV in SDHWT to ca. 200 mV, while the Keywords: R55K fi Molybdenum heme potential in SDH remains unchanged and the Mo redox potentials are not affected signi cantly in Enzyme any of these variants. Protein film voltammetry reveals a pH dependence of the electrochemical catalytic half- WT R55K VI/V Voltammetry wave potential (Ecat)of−59 mV/pH in SDH and SDH which tracks the pH dependence of the Mo redox potential.
    [Show full text]