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Journal articles on the topic 'Heme electrochemistry'

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Author: Grafiati

Published: 6 September 2023

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1

Samajdar, Rudra N., Dhivya Manogaran, S. Yashonath, and Aninda J. Bhattacharyya. "Using porphyrin–amino acid pairs to model the electrochemistry of heme proteins: experimental and theoretical investigations." Physical Chemistry Chemical Physics 20, no. 15 (2018): 10018–29. http://dx.doi.org/10.1039/c8cp00605a.

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2

Udit, Andrew K., and Harry B. Gray. "Electrochemistry of heme–thiolate proteins." Biochemical and Biophysical Research Communications 338, no. 1 (December 2005): 470–76. http://dx.doi.org/10.1016/j.bbrc.2005.08.087.

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3

Todorovic, Smilja, Catarina Barbosa, Lidia Zuccarello, and Celia M. Silveira. "Vibrational Spectro-Electrochemistry of Heme Proteins." ECS Meeting Abstracts MA2022-01, no. 14 (July 7, 2022): 963. http://dx.doi.org/10.1149/ma2022-0114963mtgabs.

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Heme proteins perform a plethora of distinct cellular functions, including e.g. electron transport (ET), energy conversion, detoxification, catalysis, signaling, and gene regulation, and as such inspire a myriad of biotechnological applications. We use resonance Raman (RR) and Surface enhanced RR (SERR) spectroscopies to probe the architecture of the heme pocket in diverse heme proteins and enzymes, which is essential for the understanding of their physiological properties as well as for the evaluation of their potential for development of the 3rd generation bioelectronic devices (1,2). Moreover, plasmonic metal that gives origin to the surface enhancement of the Raman signal of the molecules found in its close proximity can serve as an electrode, thus driving electrochemical processes. In the case of heme proteins attached to plasmonic Ag electrodes, SERR spectra selectively show vibrational bands originating from the heme moiety only, which are sensitive to spin, coordination and redox state and of the heme iron. These properties that govern the catalytic performance of heme enzymes can be monitored in potential dependent manner by SERR spectro-electrochemistry. We have demonstrated that SERR spectro-electrochemistry possesses unique capacity of to i) disentangle ET processes in multi hemic proteins, such as 28 heme containing nitrite reductase, which represent a challenge for all other experimental approaches and ii) detect subtle immobilization induced structural changes in enzymes of biotechnological interest, which e.g. in the case of cytochrome P450 may prevent their successful applications (1-4). Here we show that SERRS monitoring of electrocatalytic processes by immobilized heme peroxidases, can provide information on catalytically relevant species in situ. Several members of a recently discovered family of heme dye-decolorizing peroxidases (DyPs) that possess remarkable catalytic properties in solution and high biotechnological potential, have been immobilized on biocompatible Ag electrodes. Their structural and electrocatalytic properties studied by RR, SERR spectro-electrochemistry and electrochemistry (2). The immobilized DyP from Pseudomonas putida (PpDyP), in particular, shows native structure and outstanding analytical and catalytic parameters, and hence an exceptional potential for development of 3rd generation biosensors for H2O2 detection. In terms of sensitivity, the bioelectrodes carrying immobilized PpDyP outperform HRP based counterparts reported in the literature (2,4). The biosensor based on a PpDyP variant that harbors mutations at the second shell of the heme cavity reveals further improved storage. Our work highlights the importance of integrated, multidisciplinary approach to simultaneously evaluate the structure and catalytic properties of the enzymes, which ensures faster identification and optimization of the promising candidates for biotechnological applications. References: 1. Silveira, C. M.; Moe, E.; Fraaije, M.; Martins, L. O.; Todorovic, S. (2020). Resonance Raman view of the active site architecture in bacterial DyP-type peroxidases. RSC Advances 10, 11095. https://doi.org/10.1039/D0RA00950D 2 Barbosa, C.; Silveira, C. M.; Silva, D.; Brissos, V.; Hildebrandt, P.; Martins, L. O.; Todorovic, S. (2020). Immobilized dye-decolorizing peroxidase (DyP) and directed evolution variants for hydrogen peroxide biosensing. Biosensors and Bioelectronics 153. https://doi.org/10.1016/j.bios.2020.112055 3 Zuccarello, L.; Barbosa, C.; Galdino, E.; Lončar, N.; Silveira, C.M.; Fraaije, M.W.; Todorovic, S. (2021) SERR Spectroelectrochemistry as a Guide for Rational Design of DyP-Based Bioelectronics Devices. Int. J. Mol. Sci. 22, 7998. https://doi.org/10.3390/ijms22157998 4 Zuccarello, L.; Barbosa, C.; Todorovic, S., Silveira, C.M. (2021) Electrocatalysis by Heme Enzymes-Applications in Biosensing. Catalysts 11, 218. https://doi.org/10.3390/catal11020218

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4

Grosserueschkamp, Marc, Christoph Nowak, Wolfgang Knoll, and Renate L. C. Naumann. "Time-resolved surface-enhanced resonance Raman spectro-electrochemistry of heme proteins." Spectroscopy 24, no. 1-2 (2010): 125–29. http://dx.doi.org/10.1155/2010/815817.

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Heme proteins such as cytochrome c (cc) play a fundamental role in many biological processes. Surface-enhanced resonance Raman spectroscopy (SERRS) combined with electrochemical methods is an ideal tool to study the redox processes of heme proteins. In this context we designed a new measuring cell allowing for simultaneous electrochemical manipulation and high sensitive SERRS measurements of heme proteins. The measuring cell is based on an inverted rotating disc electrode for excitation by using a confocal Raman microscope. Furthermore, we developed a SER(R)S-active silver modified silver substrate for spectro-electrochemical applications. For this purpose silver nanoparticles (AgNPs) were adsorbed on top of a planar silver surface. The substrate was optimized for an excitation wavelength of 413 nm corresponding to the resonance frequency of heme structures. An enhancement factor of 105was achieved. The high performance of the new measuring cell in combination with the new silver substrate was demonstrated using cc as a reference system.

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5

Mie, Yasuhiro, Kumiko Sonoda, Midori Kishita, Emil Krestyn, Saburo Neya, Noriaki Funasaki, and Isao Taniguchi. "Effect of rapid heme rotation on electrochemistry of myoglobin." Electrochimica Acta 45, no. 18 (June 2000): 2903–9. http://dx.doi.org/10.1016/s0013-4686(00)00366-2.

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6

Zhou, Yinglin, Naifei Hu, Yonghuai Zeng, and James F. Rusling. "Heme Protein−Clay Films: Direct Electrochemistry and Electrochemical Catalysis." Langmuir 18, no. 1 (January 2002): 211–19. http://dx.doi.org/10.1021/la010834a.

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7

Huang, He, Naifei Hu, Yonghuai Zeng, and Gu Zhou. "Electrochemistry and electrocatalysis with heme proteins in chitosan biopolymer films." Analytical Biochemistry 308, no. 1 (September 2002): 141–51. http://dx.doi.org/10.1016/s0003-2697(02)00242-7.

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8

Shen, Li, and Naifei Hu. "Heme protein films with polyamidoamine dendrimer: direct electrochemistry and electrocatalysis." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1608, no. 1 (January 2004): 23–33. http://dx.doi.org/10.1016/j.bbabio.2003.10.007.

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9

Negahdary, Masoud, Saeed Rezaei-Zarchi, Neda Rousta, and Soheila Samei Pour. "Direct Electron Transfer of Cytochrome c on ZnO Nanoparticles Modified Carbon Paste Electrode." ISRN Biophysics 2012 (March 25, 2012): 1–6. http://dx.doi.org/10.5402/2012/937265.

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The direct electrochemistry of cytochrome c (cyt c) immobilized on a modified carbon paste electrode (CPE) was described. The electrode was modified with ZnO nanoparticles. Direct electrochemistry of cytochrome c in this paste electrode was easily achieved, and a pair of well-defined quasireversible redox peaks of a heme Fe (III)/Fe(II) couple appeared with a formal potential (E0) of −0.303 V (versus SCE) in pH 7.0 phosphate buffer solution (PBS). The fabricated modified bioelectrode showed good electrocatalytic ability for reduction of H2O2. The preparation process of the proposed biosensor was convenient, and the resulting biosensor showed high sensitivity, low detection limit, and good stability.

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10

Ma, X., Z. Sun, X. Zheng, and G. Li. "Electrochemistry and electrocatalytic properties of heme proteins incorporated in lipopolysaccharide films." Journal of Analytical Chemistry 61, no. 7 (July 2006): 669–72. http://dx.doi.org/10.1134/s1061934806070112.

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11

WANG, S., F. XIE, and G. LIU. "Direct electrochemistry and electrocatalysis of heme proteins on SWCNTs-CTAB modified electrodes." Talanta 77, no. 4 (February 15, 2009): 1343–50. http://dx.doi.org/10.1016/j.talanta.2008.09.019.

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12

Liu, Hui-Hong, Zhi-Quan Tian, Zhe-Xue Lu, Zhi-Ling Zhang, Min Zhang, and Dai-Wen Pang. "Direct electrochemistry and electrocatalysis of heme-proteins entrapped in agarose hydrogel films." Biosensors and Bioelectronics 20, no. 2 (September 2004): 294–304. http://dx.doi.org/10.1016/j.bios.2004.01.015.

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13

Li, Ye-Mei, Hui-Hong Liu, and Dai-Wen Pang. "Direct electrochemistry and catalysis of heme-proteins entrapped in methyl cellulose films." Journal of Electroanalytical Chemistry 574, no. 1 (December 2004): 23–31. http://dx.doi.org/10.1016/j.jelechem.2004.07.011.

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14

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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15

Wu, Yunhua, Qiuchan Shen, and Shengshui Hu. "Direct electrochemistry and electrocatalysis of heme-proteins in regenerated silk fibroin film." Analytica Chimica Acta 558, no. 1-2 (February 2006): 179–86. http://dx.doi.org/10.1016/j.aca.2005.11.031.

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16

Zhao, Ge, Jiu-Ju Feng, Jing-Juan Xu, and Hong-Yuan Chen. "Direct electrochemistry and electrocatalysis of heme proteins immobilized on self-assembled ZrO2 film." Electrochemistry Communications 7, no. 7 (July 2005): 724–29. http://dx.doi.org/10.1016/j.elecom.2005.04.026.

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17

Li, Ruimin, Qin Jiang, Hanjun Cheng, Guoqiang Zhang, Mingming Zhen, Daiqin Chen, Jiechao Ge, Lanqun Mao, Chunru Wang, and Chunying Shu. "G-quadruplex DNAzymes-induced highly selective and sensitive colorimetric sensing of free heme in rat brain." Analyst 139, no. 8 (2014): 1993–99. http://dx.doi.org/10.1039/c3an02025h.

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18

Sim, Sanghoon, and Noriyuki Asakura. "Analysis of a high redox potential heme in tetraheme cytochrome c3 by direct electrochemistry." Electrochemistry Communications 34 (September 2013): 161–64. http://dx.doi.org/10.1016/j.elecom.2013.05.033.

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19

Chattopadhyay, Krishnananda, and Shyamalava Mazumdar. "Direct electrochemistry of heme proteins: effect of electrode surface modification by neutral surfactants." Bioelectrochemistry 53, no. 1 (January 2001): 17–24. http://dx.doi.org/10.1016/s0302-4598(00)00092-1.

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20

Hauser, K., J. Mao, and M. R. Gunner. "pH dependence of heme electrochemistry in cytochromes investigated by multiconformation continuum electrostatic calculations." Biopolymers 74, no. 1-2 (2004): 51–54. http://dx.doi.org/10.1002/bip.20042.

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21

de Groot, Matheus T., Maarten Merkx, and Marc T. M. Koper. "Additional evidence for heme release in myoglobin-DDAB films on pyrolitic graphite." Electrochemistry Communications 8, no. 6 (June 2006): 999–1004. http://dx.doi.org/10.1016/j.elecom.2006.03.045.

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22

Gao, Zhi-Da, Hai-Feng Liu, Cheng-Yong Li, and Yan-Yan Song. "Biotemplated synthesis of Au nanoparticles–TiO2nanotube junctions for enhanced direct electrochemistry of heme proteins." Chem. Commun. 49, no. 8 (2013): 774–76. http://dx.doi.org/10.1039/c2cc38183d.

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23

Xu, Yanxia, Fang Wang, Xiaoxia Chen, and Shengshui Hu. "Direct electrochemistry and electrocatalysis of heme-protein based on N,N-dimethylformamide film electrode." Talanta 70, no. 3 (October 15, 2006): 651–55. http://dx.doi.org/10.1016/j.talanta.2006.01.030.

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24

Li, Zhen, and Naifei Hu. "Direct electrochemistry of heme proteins in their layer-by-layer films with clay nanoparticles." Journal of Electroanalytical Chemistry 558 (October 2003): 155–65. http://dx.doi.org/10.1016/s0022-0728(03)00390-5.

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25

Zhou, Yanli, Jing Wang, Lantao Liu, Rongrong Wang, Xinhe Lai, and Maotian Xu. "Interaction between Amyloid-β Peptide and Heme Probed by Electrochemistry and Atomic Force Microscopy." ACS Chemical Neuroscience 4, no. 4 (January 24, 2013): 535–39. http://dx.doi.org/10.1021/cn300231q.

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26

Novak, David, Milos Mojovic, Aleksandra Pavicevic, Martina Zatloukalova, Lenka Hernychova, Martin Bartosik, and Jan Vacek. "Electrochemistry and electron paramagnetic resonance spectroscopy of cytochrome c and its heme-disrupted analogs." Bioelectrochemistry 119 (February 2018): 136–41. http://dx.doi.org/10.1016/j.bioelechem.2017.09.011.

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27

Feng, Jiu-Ju, Ge Zhao, Jing-Juan Xu, and Hong-Yuan Chen. "Direct electrochemistry and electrocatalysis of heme proteins immobilized on gold nanoparticles stabilized by chitosan." Analytical Biochemistry 342, no. 2 (July 2005): 280–86. http://dx.doi.org/10.1016/j.ab.2005.04.040.

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28

SUZUKI, Yohei, Keisei SOWA, Yuki KITAZUMI, and Osamu SHIRAI. "The Redox Potential Measurements for Heme Moieties in Variants of D-Fructose Dehydrogenase Based on Mediator-assisted Potentiometric Titration." Electrochemistry 89, no. 4 (July 5, 2021): 337–39. http://dx.doi.org/10.5796/electrochemistry.21-00044.

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29

KOBAYASHI, Eisuke, Yo HIROSE, Toshiaki KAMACHI, Kenji TABATA, Ichiro OKURA, and Noriyuki ASAKURA. "Investigation of the Key Heme in Cytchrome c₃ to the Electron Pool Effect by Highly Sensitive EQCM Technique." Electrochemistry 80, no. 5 (2012): 312–14. http://dx.doi.org/10.5796/electrochemistry.80.312.

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30

Xu, Xin, Bozhi Tian, Song Zhang, Jilie Kong, Dongyuan Zhao, and Baohong Liu. "Electrochemistry and biosensing reactivity of heme proteins adsorbed on the structure-tailored mesoporous Nb2O5 matrix." Analytica Chimica Acta 519, no. 1 (August 2004): 31–38. http://dx.doi.org/10.1016/j.aca.2004.05.061.

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31

Topoglidis, Emmanuel, Yeni Astuti, Francine Duriaux, Michael Grätzel, and James R. Durrant. "Direct Electrochemistry and Nitric Oxide Interaction of Heme Proteins Adsorbed on Nanocrystalline Tin Oxide Electrodes." Langmuir 19, no. 17 (August 2003): 6894–900. http://dx.doi.org/10.1021/la034466h.

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32

Fleming, Barry D., Stephen G. Bell, Luet-Lok Wong, and Alan M. Bond. "The electrochemistry of a heme-containing enzyme, CYP199A2, adsorbed directly onto a pyrolytic graphite electrode." Journal of Electroanalytical Chemistry 611, no. 1-2 (December 2007): 149–54. http://dx.doi.org/10.1016/j.jelechem.2007.08.016.

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33

Suprun, Elena V., Fabiana Arduini, Danila Moscone, Giuseppe Palleschi, Victoria V. Shumyantseva, and Alexander I. Archakov. "Direct Electrochemistry of Heme Proteins on Electrodes Modified with Didodecyldimethyl Ammonium Bromide and Carbon Black." Electroanalysis 24, no. 10 (September 23, 2012): 1923–31. http://dx.doi.org/10.1002/elan.201200359.

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34

Li, Qingwen, Guoan Luo, and Jun Feng. "Direct Electron Transfer for Heme Proteins Assembled on Nanocrystalline TiO2 Film." Electroanalysis 13, no. 5 (April 2001): 359–63. http://dx.doi.org/10.1002/1521-4109(200104)13:5<359::aid-elan359>3.0.co;2-j.

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35

Shaine, M. L., W. R. Premasiri, H. M. Ingraham, R. Andino, P. Lemler, A. N. Brodeur, and L. D. Ziegler. "Surface enhanced Raman scattering for robust, sensitive detection and confirmatory identification of dried bloodstains." Analyst 145, no. 18 (2020): 6097–110. http://dx.doi.org/10.1039/d0an01132k.

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36

Nadzhafova, O. "Heme proteins sequestered in silica sol–gels using surfactants feature direct electron transfer and peroxidase activity." Electrochemistry Communications 6, no. 2 (February 2004): 205–9. http://dx.doi.org/10.1016/j.elecom.2003.11.013.

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37

Nowak, Christoph, Denise Schach, Marc Grosserüschkamp, Wolfgang Knoll, and Renate L. C. Naumann. "Cytochrome C as a benchmark system for a two-layer gold surface with improved surface-enhancement for spectro-electrochemistry." Spectroscopy 24, no. 1-2 (2010): 173–76. http://dx.doi.org/10.1155/2010/787569.

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A two-layer gold surface is developed for use with electrochemistry followed by surface-enhanced infrared absorption spectroscopy (SEIRAS) consisting of a conducting underlayer onto which Au nanoparticles (AuNPs) are grown by self-catalyzed electroless deposition. AuNPs are grown on protruding substructures of the 25 nm thin underlayer. The enhancement factor of the two-layer gold surface is controlled by the growth conditions. Cytochrome c adsorbed to a self-assembled monolayer of mercaptoethanol is used as a benchmark system for the investigation of complex heme proteins from the respiratory chain such as cytochrome c oxidase and the bc1 complex. Under optimum conditions the absorbance of the amide I band of cytochrome c is increased by a factor of 5 vs. classical SEIRAS surface. Reversible reduction/oxidation of cytochrome c on the two-layer gold surface is shown to take place by cyclic voltammetry.

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38

Ye, Tao, Ravinder Kaur, Xin Wen, Kara L. Bren, and Sean J. Elliott. "Redox Properties of Wild-Type and Heme-Binding Loop Mutants of Bacterial CytochromescMeasured by Direct Electrochemistry." Inorganic Chemistry 44, no. 24 (November 2005): 8999–9006. http://dx.doi.org/10.1021/ic051003l.

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39

Sun, Yi-Xin, and Sheng-Fu Wang. "Direct electrochemistry and electrocatalytic characteristic of heme proteins immobilized in a new sol–gel polymer film." Bioelectrochemistry 71, no. 2 (November 2007): 172–79. http://dx.doi.org/10.1016/j.bioelechem.2007.04.004.

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40

Mirčeski, Valentin, Tatyana Dzimbova, Birhan Sefer, and Gjorgji Krakutovski. "Electrochemistry of coupled electron-ion transfer of a heme-like complex in an artificial organic membrane." Bioelectrochemistry 78, no. 2 (June 2010): 147–54. http://dx.doi.org/10.1016/j.bioelechem.2009.09.006.

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41

Chen, Ting, Huayu Xiong, Wei Wen, Xiuhua Zhang, and Shengfu Wang. "Electrochemistry of heme proteins entrapped in DNA films in two imidazolium-based room temperature ionic liquids." Bioelectrochemistry 91 (June 2013): 8–14. http://dx.doi.org/10.1016/j.bioelechem.2012.11.002.

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42

Peng, Hua-Ping, Ru-Ping Liang, Li Zhang, and Jian-Ding Qiu. "General preparation of novel core–shell heme protein–Au–polydopamine–Fe3O4 magnetic bionanoparticles for direct electrochemistry." Journal of Electroanalytical Chemistry 700 (July 2013): 70–76. http://dx.doi.org/10.1016/j.jelechem.2013.04.016.

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43

Millo, Diego, Antonio Ranieri, Wynanda Koot, Cees Gooijer, and Gert van der Zwan. "Towards Combined Electrochemistry and Surface-Enhanced Resonance Raman of Heme Proteins: Improvement of Diffusion Electrochemistry of Cytochromecat Silver Electrodes Chemically Modified with 4-Mercaptopyridine." Analytical Chemistry 78, no. 15 (August 2006): 5622–25. http://dx.doi.org/10.1021/ac060807v.

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44

Hu, Naifei. "Direct electrochemistry of redox proteins or enzymes at various film electrodes and their possible applications in monitoring some pollutants." Pure and Applied Chemistry 73, no. 12 (January 1, 2001): 1979–91. http://dx.doi.org/10.1351/pac200173121979.

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Water-insoluble films modified on the surface of solid electrodes may provide a unique microenvironment for electron transfer of some redox proteins or enzymes. The film materials can be two-tail surfactants, or composites of polyion-surfactant or clay-surfactant. Both surfactant and composite films cast on surface of electrodes are self-assembled into an ordered multibilayer structure, which is very similar to the bilayer structure of biological membrane. Amphiphilic polymers can also be used for making films. Incorporated heme proteins such as myoglobin (Mb), hemoglobin (Hb), or horseradish peroxidase (HRP) in these films demonstrated reversible voltammetry. Studies of direct electrochemistry of these proteins in various films by our group are reviewed in this paper. The protein films may provide a good model for study of electron transfer process in biological systems. The electrocatalytic properties of the protein films may also be applied to monitor some pollutant substrates.

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45

Guto, Peterson M., and James F. Rusling. "Myoglobin retains iron heme and near-native conformation in DDAB films prepared from pH 5 to 7 dispersions." Electrochemistry Communications 8, no. 3 (March 2006): 455–59. http://dx.doi.org/10.1016/j.elecom.2006.01.007.

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46

Gunner, M. R., Emil Alexov, Eduardo Torres, and Samir Lipovaca. "The importance of the protein in controlling the electrochemistry of heme metalloproteins: methods of calculation and analysis." JBIC Journal of Biological Inorganic Chemistry 2, no. 1 (February 1997): 126–34. http://dx.doi.org/10.1007/s007750050116.

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47

Zhao, Liyun, Hongyun Liu, and Naifei Hu. "Assembly of layer-by-layer films of heme proteins and single-walled carbon nanotubes: electrochemistry and electrocatalysis." Analytical and Bioanalytical Chemistry 384, no. 2 (December 15, 2005): 414–22. http://dx.doi.org/10.1007/s00216-005-0204-5.

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48

Wang, Sheng-Fu, Ting Chen, Zhi-Ling Zhang, Xin-Cheng Shen, Zhe-Xue Lu, Dai-Wen Pang, and Kwok-Yin Wong. "Direct Electrochemistry and Electrocatalysis of Heme Proteins Entrapped in Agarose Hydrogel Films in Room-Temperature Ionic Liquids." Langmuir 21, no. 20 (September 2005): 9260–66. http://dx.doi.org/10.1021/la050947k.

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49

Toma, Henrique E., and Eduardo Stadler. "Electrochemical behaviour of a heme model complex in aqueous solution." Journal of Electroanalytical Chemistry and Interfacial Electrochemistry 235, no. 1-2 (October 1987): 179–87. http://dx.doi.org/10.1016/0022-0728(87)85206-3.

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50

Xu, Hui, Hua-Yu Xiong, Qing-Xiang Zeng, Li Jia, Yan Wang, and Sheng-Fu Wang. "Direct electrochemistry and electrocatalysis of heme proteins immobilized in single-wall carbon nanotubes-surfactant films in room temperature ionic liquids." Electrochemistry Communications 11, no. 2 (February 2009): 286–89. http://dx.doi.org/10.1016/j.elecom.2008.11.025.

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