Carbon Dots as Versatile Photosensitizers for Solar-Driven Catalysis with Redox Enzymes

Light-driven enzymatic catalysis is enabled by the productive coupling of a protein to a photosensitizer. Photosensitizers used in such hybrid systems are typically costly, toxic, and/or fragile, with limited chemical versatility. Carbon dots (CDs) are low-cost, nanosized light-harvesters that are attractive photosensitizers for biological systems as they are water-soluble, photostable, nontoxic, and their surface chemistry can be easily modified. We demonstrate here that CDs act as excellent light-absorbers in two semibiological photosynthetic systems utilizing either a fumarate reductase (FccA) for the solar-driven hydrogenation of fumarate to succinate or a hydrogenase (H$_{2}$ase) for reduction of protons to H$_{2}$. The tunable surface chemistry of the CDs was exploited to synthesize positively charged ammonium-terminated CDs (CD-NHMe$_{2}$$^{+}$), which were capable of transferring photoexcited electrons directly to the negatively charged enzymes with high efficiency and stability. Enzyme-based turnover numbers of 6000 mol succinate (mol FccA)$^{-1}$ and 43,000 mol H$_{2}$ (mol H$_{2}$ase)$^{-1}$ were reached after 24 h. Negatively charged carboxylate-terminated CDs (CD-CO$_{2}$$^{-}$) displayed little or no activity, and the electrostatic interactions at the CD–enzyme interface were determined to be essential to the high photocatalytic activity observed with CD-NHMe$_{2}$$^{+}$. The modular surface chemistry of CDs together with their photostability and aqueous solubility make CDs versatile photosensitizers for redox enzymes with great scope for their utilization in photobiocatalysis.This work was supported by a Cambridge Australia Poynton PhD scholarship (to G.A.M.H.), the BBSRC (BB/K010220/1 to E.R. and BB/K009885/1 to J.N.B.), an Oppenheimer PhD scholarship (to B.C.M.M.), and a Marie Curie postdoctoral fellowship (GAN 624997 to C.A.C.)

Multi-heme Cytochromes in Shewanella oneidensis MR-1:Structures, functions and opportunities

Multi-heme cytochromes are employed by a range of microorganisms to transport electrons over distances of up to tens of nanometers. Perhaps the most spectacular utilization of these proteins is in the reduction of extracellular solid substrates, including electrodes and insoluble mineral oxides of Fe(III) and Mn(III/IV), by species of Shewanella and Geobacter. However, multi-heme cytochromes are found in numerous and phylogenetically diverse prokaryotes where they participate in electron transfer and redox catalysis that contributes to biogeochemical cycling of N, S and Fe on the global scale. These properties of multi-heme cytochromes have attracted much interest and contributed to advances in bioenergy applications and bioremediation of contaminated soils. Looking forward there are opportunities to engage multi-heme cytochromes for biological photovoltaic cells, microbial electrosynthesis and developing bespoke molecular devices. As a consequence it is timely to review our present understanding of these proteins and we do this here with a focus on the multitude of functionally diverse multi-heme cytochromes in Shewanella oneidensis MR-1. We draw on findings from experimental and computational approaches which ideally complement each other in the study of these systems: computational methods can interpret experimentally determined properties in terms of molecular structure to cast light on the relation between structure and function. We show how this synergy has contributed to our understanding of multi-heme cytochromes and can be expected to continue to do so for greater insight into natural processes and their informed exploitation in biotechnologies

Silicon containing electroconductive polymers and structures made therefrom

An electropolymerized film comprised of polymers and copolymers of a monomer is formed on the surface of an anode. The finished structures have superior electrical and mechanical properties for use in applications such as electrostatic dissipation and for the reduction of the radar cross section of advanced aircraft

Electronic structure of an iron porphyrin derivative on Au(1 1 1)

Surface-bound porphyrins are promising candidates for molecular switches, electronics and spintronics. Here, we studied the structural and the electronic properties of Fe-tetra-pyridil-porphyrin adsorbed on Au(1 1 1) in the monolayer regime. We combined scanning tunneling microscopy/spectroscopy, ultraviolet photoemission, and two-photon photoemission to determine the energy levels of the frontier molecular orbitals. We also resolved an excitonic state with a binding energy of 420 meV, which allowed us to compare the electronic transport gap with the optical gap

Atomic Ensemble Effects and Non-Covalent Interactions at the Electrode–Electrolyte Interface

Peer reviewedPublisher PD

Mechanical rolling formation of interpenetrated lithium metal/lithium tin alloy foil for ultrahigh-rate battery anode

To achieve good rate capability of lithium metal anodes for high-energy-density batteries, one fundamental challenge is the slow lithium diffusion at the interface. Here we report an interpenetrated, three-dimensional lithium metal/lithium tin alloy nanocomposite foil realized by a simple calendering and folding process of lithium and tin foils, and spontaneous alloying reactions. The strong affinity between the metallic lithium and lithium tin alloy as mixed electronic and ionic conducting networks, and their abundant interfaces enable ultrafast charger diffusion across the entire electrode. We demonstrate that a lithium/lithium tin alloy foil electrode sustains stable lithium stripping/plating under 30mAcm(-2) and 5mAhcm(-2) with a very low overpotential of 20mV for 200 cycles in a commercial carbonate electrolyte. Cycled under 6C (6.6mAcm(-2)), a 1.0mAhcm(-2) LiNi0.6Co0.2Mn0.2O2 electrode maintains a substantial 74% of its capacity by pairing with such anode

Modification of bacterial cell membrane to accelerate decolorization of textile wastewater effluent using microbial fuel cells: role of gamma radiation

The aim of the present work was to increase bacterial adhesion on anode via inducing membrane modifications to enhance textile wastewater treatment in Microbial Fuel Cell (MFC). Real textile wastewater was used in mediator-less MFCs for bacterial enrichment. The enriched bacteria were pre-treated by exposure to 1 KGy gamma radiation and were tested in MFC setup. Bacterial cell membrane permeability and cell membrane charges were measured using noninvasive dielectric spectroscopy measurements. The results show that pre-treatment using gamma radiation resulted in biofilm formation and increased cell permeability and exopolysaccharide production; this was reflected in both MFC performance (average voltage 554.67 mV) and decolorization (96.42%) as compared to 392.77 mV and 60.76% decolorization for non-treated cells. At the end of MFC operation, cytotoxicity test was performed for treated wastewater using a dermal cell line, the results obtained show a decrease in toxicity from 24.8 to 0 (v/v%) when cells were exposed to gamma radiation. Fourier-transform infrared (FTIR) spectroscopy showed an increase in exopolysaccharides in bacterial consortium exposed to increasing doses of gamma radiation suggesting that gamma radiation increased exopolysaccharide production, providing transient media for electron transfer and contributing to accelerating MFC performance. Modification of bacterial membrane prior to MFC operation can be considered highly effective as a pre-treatment tool that accelerates MFC performance

The influence of the shape of Au nanoparticles on the catalytic current of fructose dehydrogenase

Graphite electrodes were modified with triangular (AuNTrs) or spherical (AuNPs) nanoparticles and further modified with fructose dehydrogenase (FDH). The present study reports the effect of the shape of these nanoparticles (NPs) on the catalytic current of immobilized FDH pointing out the different contributions on the mass transfer–limited and kinetically limited currents. The influence of the shape of the NPs on the mass transfer–limited and the kinetically limited current has been proved by using two different methods: a rotating disk electrode (RDE) and an electrode mounted in a wall jet flow-through electrochemical cell attached to a flow system. The advantages of using the wall jet flow system compared with the RDE system for kinetic investigations are as follows: no need to account for substrate consumption, especially in the case of desorption of enzyme, and studies of product-inhibited enzymes. The comparison reveals that virtually identical results can be obtained using either of the two techniques. The heterogeneous electron transfer (ET) rate constants (kS) were found to be 3.8 ± 0.3 s−1 and 0.9 ± 0.1 s−1, for triangular and spherical NPs, respectively. The improvement observed for the electrode modified with AuNTrs suggests a more effective enzyme-NP interaction, which can allocate a higher number of enzyme molecules on the electrode surface

Electron transfer in an acidophilic bacterium: interaction between a diheme cytochrome and a cupredoxin

Acidithiobacillus ferrooxidans, a chemolithoautotrophic Gram-negative bacterium, has a remarkable ability to obtain energy from ferrous iron oxidation at pH 2. Several metalloproteins have been described as being involved in this respiratory chain coupling iron oxidation with oxygen reduction. However, their properties and physiological functions remain largely unknown, preventing a clear understanding of the global mechanism. In this work, we focus on two metalloproteins of this respiratory pathway, a diheme cytochrome c4 (Cyt c4) and a green copper protein (AcoP) of unknown function. We first demonstrate the formation of a complex between these two purified proteins, which allows homogeneous intermolecular electron-transfer in solution. We then mimic the physiological interaction between the two partners by replacing one at a time with electrodes displaying different chemical functionalities. From the electrochemical behavior of individual proteins, we show that, while electron transfer on AcoP requires weak electrostatic interaction, electron transfer on Cyt c4 tolerates different charge and hydrophobicity conditions, suggesting a pivotal role of this protein in the metabolic chain. The electrochemical study of the proteins incubated together demonstrates an intermolecular electron transfer involving the protein complex, in which AcoP is reduced through the high potential heme of Cyt c4. Modelling of the electrochemical signals at different scan rates allows us to estimate the rate constant of this intermolecular electron transfer in the range of a few s−1. Possible routes for electron transfer in the acidophilic bacterium are deduced