Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:6.2.1.1 (ACS)
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Sulfite oxidase is a mitochondria-located molybdenum-containing enzyme catalyzing the oxidation of sulfite to sulfate in the amino acid and lipid metabolism. Therefore, it plays a major role in detoxification processes, where defects in the enzyme cause a severe infant disease leading to early death with no efficient or cost-effective therapy in sight. Here we report that molybdenum trioxide (MoO3) nanoparticles display an intrinsic biomimetic sulfite oxidase activity under physiological conditions, and, functionalized with a customized bifunctional ligand containing dopamine as anchor group and triphenylphosphonium ion as targeting agent, they selectively target the mitochondria while being highly dispersible in aqueous solutions. Chemically induced sulfite oxidase knockdown cells treated with MoO3 nanoparticles recovered their sulfite oxidase activity in vitro, which makes MoO3 nanoparticles a potential therapeutic for sulfite oxidase deficiency and opens new avenues for cost-effective therapies for gene-induced deficiencies.
ACS Nano 2014 May 27
PMID:Molybdenum trioxide nanoparticles with intrinsic sulfite oxidase activity. 2470 61

The bioelectrocatalytic sulfite oxidation by human sulfite oxidase (hSO) on indium tin oxide (ITO) is reported, which is facilitated by functionalizing of the electrode surface with polyethylenimine (PEI)-entrapped CdS nanoparticles and enzyme. hSO was assembled onto the electrode with a high surface loading of electroactive enzyme. In the presence of sulfite but without additional mediators, a high bioelectrocatalytic current was generated. Reference experiments with only PEI showed direct electron transfer and catalytic activity of hSO, but these were less pronounced. The application of the polyelectrolyte-entrapped quantum dots (QDs) on ITO electrodes provides a compatible surface for enzyme binding with promotion of electron transfer. Variations of the buffer solution conditions, e.g., ionic strength, pH, viscosity, and the effect of oxygen, were studied in order to understand intramolecular and heterogeneous electron transfer from hSO to the electrode. The results are consistent with a model derived for the enzyme by using flash photolysis in solution and spectroelectrochemistry and molecular dynamic simulations of hSO on monolayer-modified gold electrodes. Moreover, for the first time a photoelectrochemical electrode involving immobilized hSO is demonstrated where photoexcitation of the CdS/hSO-modified electrode lead to an enhanced generation of bioelectrocatalytic currents upon sulfite addition. Oxidation starts already at the redox potential of the electron transfer domain of hSO and is greatly increased by application of a small overpotential to the CdS/hSO-modified ITO.
ACS Appl Mater Interfaces 2015 Sep 30
PMID:Effective Electrochemistry of Human Sulfite Oxidase Immobilized on Quantum-Dots-Modified Indium Tin Oxide Electrode. 2635 59

Local surface plasmon resonance (LSPR)-enhanced catalysis has brought a substantial amount of opportunities across various disciplines such as photocatalysis, photodetection, and photothermal therapeutics. Plasmon-induced photothermal and hot carriers effects have also been utilized to activate the enzyme-like reactions. Compared with natural enzymes, the relatively low catalytic performance of nanozymes severely hampered the potential applications in the field of biomedicine. For these issues mentioned above, herein, we demonstrate a highly efficient sulfite oxidase (SuOx) mimetic performance of plasmonic monolayer MoOx (ML-MoOx) upon LSPR excitation. We also established that the considerable photothermal effect and the injection of hot carriers induced by LSPR are responsible for promoting the SuOx activity of ML-MoOx. The high transient local temperature on the surface of ML-MoOx generated by the photothermal effect facilitates to impact the reaction velocity and feed the SuOx-like activity, while the generation of hot carriers which are suggested as predominant effects catalyzes the oxidation of sulfite to sulfate through significantly decreasing the activation energy for the SuOx-like reaction. These investigations present a contribution to the basic understanding of plasmon-enhanced enzyme-like reaction and provided an insight into the optimization of the SuOx mimetic performance of nanomaterials.
ACS Appl Mater Interfaces 2020 Apr 29
PMID:Hot Carriers and Photothermal Effects of Monolayer MoOx for Promoting Sulfite Oxidase Mimetic Activity. 3227 33