The Reversible Electrochemical Interconversion of Formate and CO by Formate Dehydrogenase from .

The bacterial molybdenum (Mo)-containing formate dehydrogenase (FdsDABG) from is a soluble NAD-dependent enzyme belonging to the DMSO reductase family. The holoenzyme is complex and possesses nine redox-active cofactors including a bis(molybdopterin guanine dinucleotide) (bis-MGD) active site, seven iron-sulfur clusters, and 1 equiv of flavin mononucleotide (FMN). FdsDABG catalyzes the two-electron oxidation of HCOO (formate) to CO and reversibly reduces CO to HCOO under physiological conditions close to its thermodynamic redox potential.

Synthesis, properties and potential applications of photoluminescent carbon nanoparticles: A review.

Photoluminescent-carbon nanoparticles (PL-CNPs) are a new class of materials that received immense interest among researchers due to their distinct characteristics, including photoluminescence, high surface-to-volume ratio, low cost, ease of synthesis, high quantum yield, and biocompatibility. By exploiting these outstanding properties, many studies have been reported on its utility as sensors, photocatalysts, probes for bio-imaging, and optoelectronics applications. From clinical applications to point-of-care test devices, drug loading to tracking of drug delivery, and other research innovations demonstrated PL-CNPs as an emerging material that could substitute conventional approaches.

Electrocatalytic Aldehyde Oxidation by a Tungsten Dependent Aldehyde Oxidoreductase from Aromatoleum Aromaticum.

In contrast to their molybdenum dependent relatives, tungsten enzymes operate at significantly lower redox potentials, and in some cases they can carry out reversible redox transformations of their substrates and products. Still, the electrochemical properties of W enzymes have received much less attention than their Mo relatives. Herein we analyse the tungsten enzyme aldehyde oxidoreductase (AOR) from the mesophilic bacterium Aromatoleum aromaticum which has been immobilised on a glassy carbon working electrode.

Catalytic electrochemistry of the bacterial Molybdoenzyme YcbX.

Molybdenum-dependent enzymes that can reduce N-hydroxylated substrates (e.g. N-hydroxyl-purines, amidoximes) are found in bacteria, plants and vertebrates.

Recent Developments in Carbon-Based Nanocomposites for Fuel Cell Applications: A Review.

Carbon-based nanocomposites have developed as the most promising and emerging materials in nanoscience and technology during the last several years. They are microscopic materials that range in size from 1 to 100 nanometers. They may be distinguished from bulk materials by their size, shape, increased surface-to-volume ratio, and unique physical and chemical characteristics.

Recent Advances in Nanoscale Based Electrocatalysts for Metal-Air Battery, Fuel Cell and Water-Splitting Applications: An Overview.

Metal-air batteries and fuel cells are considered the most promising highly efficient energy storage systems because they possess long life cycles, high carbon monoxide (CO) tolerance, and low fuel crossover ability. The use of energy storage technology in the transport segment holds great promise for producing green and clean energy with lesser greenhouse gas (GHG) emissions. In recent years, nanoscale based electrocatalysts have shown remarkable electrocatalytic performance towards the construction of sustainable energy-related devices/applications, including fuel cells, metal-air battery and water-splitting processes.

Electrochemically driven catalysis of the bacterial molybdenum enzyme YiiM.

The Mo-dependent enzyme YiiM enzyme from Escherichia coli is a member of the sulfite oxidase family and shares many similarities with the well-studied human mitochondrial amidoxime reducing component (mARC). We have investigated YiiM catalysis using electrochemical and spectroscopic methods. EPR monitored redox potentiometry found the active site redox potentials to be Mo -0.

Recent Progress in the Development of Advanced Functionalized Electrodes for Oxygen Evolution Reaction: An Overview.

Presently, the global energy demand for increasing clean and green energy consumption lies in the development of low-cost, sustainable, economically viable and eco-friendly natured electrochemical conversion process, which is a significant advancement in different morphological types of advanced electrocatalysts to promote their electrocatalytic properties. Herein, we overviewed the recent advancements in oxygen evolution reactions (OERs), including easy electrode fabrication and significant action in water-splitting devices. To date, various synthetic approaches and modern characterization techniques have effectively been anticipated for upgraded OER activity.

High-Efficiency of Bi-Functional-Based Perovskite Nanocomposite for Oxygen Evolution and Oxygen Reduction Reaction: An Overview.

High efficient, low-cost and environmentally friendly-natured bi-functional-based perovskite electrode catalysts (BFPEC) are receiving increasing attention for oxygen reduction/oxygen evolution reaction (ORR/OER), playing an important role in the electrochemical energy conversion process using fuel cells and rechargeable batteries. Herein, we highlighted the different kinds of synthesis routes, morphological studies and electrode catalysts with A-site and B-site substitution co-substitution, generating oxygen vacancies studies for boosting ORR and OER activities. However, perovskite is a novel type of oxide family, which shows the state-of-art electrocatalytic performances in energy storage device applications.

Active site architecture reveals coordination sphere flexibility and specificity determinants in a group of closely related molybdoenzymes.

MtsZ is a molybdenum-containing methionine sulfoxide reductase that supports virulence in the human respiratory pathogen Haemophilus influenzae (Hi). HiMtsZ belongs to a group of structurally and spectroscopically uncharacterized S-/N-oxide reductases, all of which are found in bacterial pathogens. Here, we have solved the crystal structure of HiMtsZ, which reveals that the HiMtsZ substrate-binding site encompasses a previously unrecognized part that accommodates the methionine sulfoxide side chain via interaction with His182 and Arg166.

Deconstructing the electron transfer chain in a complex molybdoenzyme: Assimilatory nitrate reductase from Neurospora crassa.

Nitrate reductase (NR) from the fungus Neurospora crassa is a complex homodimeric metallo-flavoenzyme, where each protomer contains three distinct domains; the catalytically active terminal molybdopterin cofactor, a central heme-containing domain, and an FAD domain which binds with the natural electron donor NADPH. Here, we demonstrate the catalytic voltammetry of variants of N. crassa NRs on a modified Au electrode with the electrochemically reduced forms of benzyl viologen (BV) and anthraquinone sulfonate (AQS) acting as artificial electron donors.

Highly Stable Passive Wireless Sensor for Protease Activity Based on Fatty Acid-Coupled Gelatin Composite Films.

Proteases are often used as biomarkers of many pathologies as well as of microbial contamination and infection. Therefore, extensive efforts are devoted to the development of protease sensors. Some applications would benefit from wireless monitoring of proteolytic activity at minimal cost, e.

The oxidation-reduction and electrocatalytic properties of CO dehydrogenase from Oligotropha carboxidovorans.

CO dehydrogenase (CODH) from the Gram-negative bacterium Oligotropha carboxidovorans is a complex metalloenzyme from the xanthine oxidase family of molybdenum-containing enzymes, bearing a unique binuclear Mo-S-Cu active site in addition to two [2Fe-2S] clusters (FeSI and FeSII) and one equivalent of FAD. CODH catalyzes the oxidation of CO to CO with the concomitant introduction of reducing equivalents into the quinone pool, thus enabling the organism to utilize CO as sole source of both carbon and energy. Using a variety of EPR monitored redox titrations and spectroelectrochemistry, we report the redox potentials of CO dehydrogenase at pH 7.

Electrocatalysis of a Europium-Dependent Bacterial Methanol Dehydrogenase with Its Physiological Electron-Acceptor Cytochrome c.

We report the first electrochemical study of a lanthanoid-dependent methanol dehydrogenase (Eu-MDH) from the acidophilic verrucomicrobial methanotroph Methylacidiphilum fumariolicum SolV with its own physiological cytochrome c electron acceptor. Eu-MDH harbours a redox active 2,7,9-tricarboxypyrroloquinoline quinone (PQQ) cofactor which is non-covalently bound but coordinates trivalent lanthanoid elements including Eu . Eu-MDH and the cytochrome were co-adsorbed with the biopolymer chitosan and cast onto a mercaptoundecanol (MU) monolayer modified Au working electrode.

Electrocatalytic Hydroxylation of Sterols by Steroid C25 Dehydrogenase from Sterolibacterium denitrificans.

The electrochemically driven catalysis of the complex molybdoenzyme steroid C25 dehydrogenase (S25DH) from the β-Proteobacterium Sterolibacterium denitrificans is reported. S25DH catalyses the oxygen-independent regioselective hydroxylation of the tertiary C25 atom of sterols and also their derivatives. Cholest-4-en-3-one is a native substrate for S25DH, which produces 25-hydroxycholest-4-en-3-one as a product of catalytic turnover.

The central active site arginine in sulfite oxidizing enzymes alters kinetic properties by controlling electron transfer and redox interactions.

A central conserved arginine, first identified as a clinical mutation leading to sulfite oxidase deficiency, is essential for catalytic competency of sulfite oxidizing molybdoenzymes, but the molecular basis for its effects on turnover and substrate affinity have not been fully elucidated. We have used a bacterial sulfite dehydrogenase, SorT, which lacks an internal heme group, but transfers electrons to an external, electron accepting cytochrome, SorU, to investigate the molecular functions of this arginine residue (Arg78). Assay of the SorT Mo centre catalytic competency in the absence of SorU showed that substitutions in the central arginine (R78Q, R78K and R78M mutations) only moderately altered SorT catalytic properties, except for R78M which caused significant reduction in SorT activity.

A Nanoporous Cytochrome c Film with Highly Ordered Porous Structure for Sensing of Toxic Vapors.

Creating well-ordered nanoporosity in biomolecules promises stability and activity, offering access to an even wider range of application possibilities. Here, the preparation of nanoporous protein films containing cytochrome c protein molecules is reported through a soft-templating strategy using polystyrene (PS) spheres of different sizes as templates. The stability of the cytochrome c film is demonstrated through electrochemistry studies to show a reusable nature of these films over a long period of time.

Chitosan-Promoted Direct Electrochemistry of Human Sulfite Oxidase.

Direct electrochemistry of human sulfite oxidase (HSO) has been achieved on carboxylate-terminated self-assembled monolayers cast on a Au working electrode in the presence of the promoter chitosan. The modified electrode facilitates a well-defined nonturnover redox response from the heme cofactor (Fe) in 750 mM Tris, MOPS, and bicine buffer solutions. The formal redox potential of the nonturnover response varies slightly depending on the nature of the thiol monolayer on the Au electrode.

Direct electrochemistry of nitrate reductase from the fungus Neurospora crassa.

We report the first direct (unmediated) catalytic electrochemistry of a eukaryotic nitrate reductase (NR). NR from the filamentous fungus Neurospora crassa, is a member of the mononuclear molybdenum enzyme family and contains a Mo, heme and FAD cofactor which are involved in electron transfer from NAD(P)H to the (Mo) active site where reduction of nitrate to nitrite takes place. NR was adsorbed on an edge plane pyrolytic graphite (EPG) working electrode.

Engineering PQQ-glucose dehydrogenase into an allosteric electrochemical Ca(2+) sensor.

Electrochemical biosensors convert biological events to an electrical current. To date most electrochemical biosensors exploit activities of naturally occurring enzymes. Here we demonstrated that insertion of a calmodulin domain into the redox enzyme PQQ-glucose dehydrogenase resulted in a selective Ca(2+) biosensor that could be used to rapidly measure Ca(2+) concentrations in human biological fluids.

Electrocatalytic hydrocarbon hydroxylation by ethylbenzene dehydrogenase from Aromatoleum aromaticum.

We report the electrocatalytic activity of ethylbenzene dehydrogenase (EBDH) from the β-proteobacterium Aromatoleum aromaticum. EBDH is a complex 155 kDa heterotrimeric molybdenum/iron-sulfur/heme protein which catalyzes the enantioselective hydroxylation of nonactivated ethylbenzene to (S)-1-phenylethanol without molecular oxygen as cosubstrate. Furthermore, it oxidizes a wide range of other alkyl-substituted aromatic and heterocyclic compounds to their secondary alcohols.

A sensitive and stable amperometric nitrate biosensor employing Arabidopsis thaliana nitrate reductase.

Nitrate reductase (NR) from the plant Arabidopsis thaliana has been employed in the development of an amperometric nitrate biosensor that functions at physiological pH. The anion anthraquinone-2-sulfonate (AQ) is used as an effective artificial electron transfer partner for NR at a glassy carbon (GC) electrode. Nitrate is enzymatically reduced to nitrite and the oxidized form of NR is electrochemically reduced by the hydroquinone form of the mediator (AQH2).

Catalytic voltammetry of the molybdoenzyme sulfite dehydrogenase from Sinorhizobium meliloti.

Sulfite dehydrogenase from the soil bacterium Sinorhizobium meliloti (SorT) is a periplasmic, homodimeric molybdoenzyme with a molecular mass of 78 kDa. It differs from most other well studied sulfite oxidizing enzymes, as it bears no heme cofactor. SorT does not readily reduce ferrous horse heart cytochrome c which is the preferred electron acceptor for vertebrate sulfite oxidases.

The tachykinin peptide neurokinin B binds copper(I) and silver(I) and undergoes quasi-reversible electrochemistry: towards a new function for the peptide in the brain.

The tachykinin neuropeptide family, which includes substance P and neurokinin B, is involved in a wide array of biological functions. Among these is the ability to protect against the neurotoxic processes in Alzheimer's Disease, but the mechanisms driving neuroprotection remain unclear. Dysregulation of metal ions, particularly copper, iron and zinc is a common feature of Alzheimer's Disease, and other amyloidogenic disorders.

Electrochemically driven catalysis of Rhizobium sp. NT-26 arsenite oxidase with its native electron acceptor cytochrome c552.

We describe the catalytic voltammograms of the periplasmic arsenite oxidase (Aio) from the chemolithoautotrophic bacterium Rhizobium sp. str. NT-26 that oxidizes arsenite to arsenate.