Theoretical and experimental studies of electron transfer in electrochemical and bioelectrochemical systems: Foreword

2021 ◽  
pp. 139400
Author(s):  
Edmond Magner ◽  
Bingwei Mao ◽  
Richard Nichols ◽  
Xinxin Xiao
2016 ◽  
Vol 82 (16) ◽  
pp. 5026-5038 ◽  
Author(s):  
Erick M. Bosire ◽  
Lars M. Blank ◽  
Miriam A. Rosenbaum

ABSTRACTPseudomonas aeruginosais an important, thriving member of microbial communities of microbial bioelectrochemical systems (BES) through the production of versatile phenazine redox mediators. Pure culture experiments with a model strain revealed synergistic interactions ofP. aeruginosawith fermenting microorganisms whereby the synergism was mediated through the shared fermentation product 2,3-butanediol. Our work here shows that the behavior and efficiency ofP. aeruginosain mediated current production is strongly dependent on the strain ofP. aeruginosa. We compared levels of phenazine production by the previously investigated model strainP. aeruginosaPA14, the alternative model strainP. aeruginosaPAO1, and the BES isolatePseudomonassp. strain KRP1 with glucose and the fermentation products 2,3-butanediol and ethanol as carbon substrates. We found significant differences in substrate-dependent phenazine production and resulting anodic current generation for the three strains, with the BES isolate KRP1 being overall the best current producer and showing the highest electrochemical activity with glucose as a substrate (19 μA cm−2with ∼150 μg ml−1phenazine carboxylic acid as a redox mediator). Surprisingly,P. aeruginosaPAO1 showed very low phenazine production and electrochemical activity under all tested conditions.IMPORTANCEMicrobial fuel cells and other microbial bioelectrochemical systems hold great promise for environmental technologies such as wastewater treatment and bioremediation. While there is much emphasis on the development of materials and devices to realize such systems, the investigation and a deeper understanding of the underlying microbiology and ecology are lagging behind. Physiological investigations focus on microorganisms exhibiting direct electron transfer in pure culture systems. Meanwhile, mediated electron transfer with natural redox compounds produced by, for example,Pseudomonas aeruginosamight enable an entire microbial community to access a solid electrode as an alternative electron acceptor. To better understand the ecological relationships between mediator producers and mediator utilizers, we here present a comparison of the phenazine-dependent electroactivities of threePseudomonasstrains. This work forms the foundation for more complex coculture investigations of mediated electron transfer in microbial fuel cells.


2012 ◽  
Vol 40 (6) ◽  
pp. 1330-1335 ◽  
Author(s):  
Kamrul Hasan ◽  
Sunil A. Patil ◽  
Dónal Leech ◽  
Cecilia Hägerhäll ◽  
Lo Gorton

Electrochemical communication between micro-organisms and electrodes is the integral and fundamental part of BESs (bioelectrochemical systems). The immobilization of bacterial cells on the electrode and ensuring efficient electron transfer to the electrode via a mediator are decisive features of mediated electrochemical biosensors. Notably, mediator-based systems are essential to extract electrons from the non-exoelectrogens, a major group of microbes in Nature. The advantage of using polymeric mediators over diffusible mediators led to the design of osmium redox polymers. Their successful use in enzyme-based biosensors and BFCs (biofuel cells) paved the way for exploring their use in microbial BESs. The present mini-review focuses on osmium-bound redox systems used to date in microbial BESs and their role in shuttling electrons from viable microbial cells to electrodes.


2001 ◽  
Vol 34 (4) ◽  
pp. 563-679 ◽  
Author(s):  
Arieh Warshel ◽  
William W. Parson

1. Introduction 5632. Obtaining rate constants from molecular-dynamics simulations 5642.1 General relationships between quantum electronic structures and reaction rates 5642.2 The transition-state theory (TST) 5692.3 The transmission coefficient 5723. Simulating biological electron-transfer reactions 5753.1 Semi-classical surface-hopping and the Marcus equation 5753.2 Treating quantum mechanical nuclear tunneling by the dispersed-polaron/spin-boson method 5803.3 Density-matrix treatments 5833.4 Charge separation in photosynthetic bacterial reaction centers 5844. Light-induced photoisomerizations in rhodopsin and bacteriorhodopsin 5965. Energetics and dynamics of enzyme reactions 6145.1 The empirical-valence-bond treatment and free-energy perturbation methods 6145.2 Activation energies are decreased in enzymes relative to solution, often by electrostatic effects that stabilize the transition state 6205.3 Entropic effects in enzyme catalysis 6275.4 What is meant by dynamical contributions to catalysis? 6345.5 Transmission coefficients are similar for corresponding reactions in enzymes and water 6365.6 Non-equilibrium solvation effects contribute to catalysis mainly through Δg[Dagger], not the transmission coefficient 6415.7 Vibrationally assisted nuclear tunneling in enzyme catalysis 6485.8 Diffusive processes in enzyme reactions and transmembrane channels 6516. Concluding remarks 6587. Acknowledgements 6588. References 658Obtaining a detailed understanding of the dynamics of a biochemical reaction is a formidable challenge. Indeed, it might appear at first sight that reactions in proteins are too complex to analyze microscopically. At room temperature, even a relatively small protein can have as many as 1034 accessible conformational states (Dill, 1985). In many cases, however, we have detailed structural information about the active site of an enzyme, whereas such information is missing for corresponding chemical systems in solution. The atomic coordinates of the chromophore in bacteriorhodopsin, for example, are known to a resolution of 1–2 Å. In addition, experimental studies of biological processes such as photoisomerization and electron transfer have provided a wealth of detailed information that eventually may make some of these processes classical problems in chemical physics as well as biology.


2010 ◽  
Vol 114 (21) ◽  
pp. 6284-6297 ◽  
Author(s):  
Alexey L. Kaledin ◽  
Zhuangqun Huang ◽  
Qiushi Yin ◽  
Emma L. Dunphy ◽  
Edwin C. Constable ◽  
...  

2018 ◽  
Vol 264 ◽  
pp. 387-390 ◽  
Author(s):  
Ja Hyun Lee ◽  
Dong Sup Kim ◽  
Ji Hyun Yang ◽  
Youngsang Chun ◽  
Hah Young Yoo ◽  
...  

2012 ◽  
Vol 47 (12) ◽  
pp. 1707-1714 ◽  
Author(s):  
Yonggang Yang ◽  
Meiying Xu ◽  
Jun Guo ◽  
Guoping Sun

2019 ◽  
Author(s):  
N.L. Costa ◽  
B. Hermann ◽  
V. Fourmond ◽  
M. Faustino ◽  
M. Teixeira ◽  
...  

AbstractExtracellular electron transfer is the key process underpinning the development of bioelectrochemical systems for the production of energy or added-value compounds. Thermincola potens JR is a promising Gram-positive bacterium to be used in these systems because it is thermophilic. In this paper we describe the structural and functional properties of the nonaheme cytochrome OcwA, which is the terminal reductase of this organism. The structure of OcwA, determined at 2.2Å resolution shows that the overall-fold and organization of the hemes are not related to other metal reductases and instead are similar to that of multiheme cytochromes involved in the biogeochemical cycles of nitrogen and sulfur. We show that, in addition to solid electron acceptors, OcwA can also reduce soluble electron shuttles and oxyanions. These data reveal that OcwA can take the role of a respiratory ‘swiss-army knife’ allowing this organism to grow in environments with rapidly changing availability of terminal electron acceptors without the need for transcriptional regulation and protein synthesis.ImportanceThermophilic Gram-positive organisms were recently shown to be a promising class of organisms to be used in bioelectrochemical systems for the production of electrical energy. These organisms present a thick peptidoglycan layer that was thought to preclude them to perform extracellular electron transfer (i.e. exchange catabolic electrons with solid electron acceptors outside of the cell). In this manuscript we describe the structure and functional mechanisms of the multiheme cytochrome OcwA, the terminal reductase of the Gram-positive bacterium Thermincola potens JR found at the cell surface of this organism. The results presented here show that this protein is unrelated with terminal reductases found at the cell surface of other electroactive organisms. Instead, OcwA is similar to terminal reductases of soluble electron acceptors. Our data reveals that terminal oxidoreductases of soluble and insoluble substrates are evolutionarily related, providing novel insights into the evolutionary pathway of multiheme cytochromes.


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