Redox enzymes in bioelectronic devices usually lack direct electrical contact with electrodes, owing to the spatial separation of their redox centers from the conductive surfaces by the protein shells. The reconstitution of apo-enzymes on cofactor-functionalized nanostructures associated with electrodes provides a means to align the biocatalysts on the conductive surface and to electrically contact redox enzymes with electrodes. The reconstitution of apo-enzymes on cofactor-functionalized gold nanoparticles or carbon nanotubes has led to effective electrical communication between the redox proteins and the electrodes. Alternatively, the reconstitution of redox enzymes on molecular wires that enable electron tunneling or dynamic charge shuttling represent supramolecular biocatalytic nanostructures exhibiting electrical contact. The bioelectrocatalytic activities of the electrically wired reconstituted enzymes on electrodes have allowed the development of amperometric biosensors and biofuel cell elements.
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http://dx.doi.org/10.1016/j.copbio.2006.10.008 | DOI Listing |
BMC Bioinformatics
January 2025
Department of Chemistry, University of Louisiana at Lafayette, Lafayette, LA, 70504, USA.
Background: All chemical forms of energy and oxygen on Earth are generated via photosynthesis where light energy is converted into redox energy by two photosystems (PS I and PS II). There is an increasing number of PS I 3D structures deposited in the Protein Data Bank (PDB). The Triangular Spatial Relationship (TSR)-based algorithm converts 3D structures into integers (TSR keys).
View Article and Find Full Text PDFMikrochim Acta
January 2025
Department of General Surgery, Hui Ya Hospital of The First Affiliated Hospital, Sun Yat-Sen University, Huizhou, 516081, Guangdong, China.
Self-supported ultrathin PtRuMoCoNi high-entropy alloy nanowires (HEANWs) were synthesized by a one-pot co-reduction method, whose peroxidase (POD)-like activity and catalytic mechanism were elaborated in detail. As expected, the PtRuMoCoNi HEANWs showed excellent POD-like activity. It can quickly catalyze the oxidization of colorless 3,3',5,5'-tetramethylbenzidine (TMB) to blue TMB through decomposition of HO to superoxide radicals.
View Article and Find Full Text PDFPhotosynth Res
January 2025
Department of Chemistry, Graduate School of Science and Technology, Proteo-Science Research Center, Ehime University, Bunkyo-cho, Matsuyama, Ehime, 790-8577, Japan.
The active site for water oxidation in photosystem II (PSII) comprises a MnCaO cluster adjacent to a redox-active tyrosine residue (Tyr). During the water-splitting process, the enzyme transitions through five sequential oxidation states (S to S), with O evolution occurring during the STyr· to STyr transition. Chloride also plays a role in this mechanism.
View Article and Find Full Text PDFSkelet Muscle
January 2025
Department of Anesthesia and Critical Care, The Second Affiliated Hospital of Wenzhou Medical University, Wenzhou, China.
Background: Duchenne muscular dystrophy (DMD) is a prevalent, fatal degenerative muscle disease with no effective treatments. Mdx mouse model of DMD exhibits impaired muscle performance, oxidative stress, and dysfunctional autophagy. Although antioxidant treatments may improve the mdx phenotype, the precise molecular mechanisms remain unclear.
View Article and Find Full Text PDFMikrochim Acta
January 2025
College of Medical Technology, Chengdu University of Traditional Chinese Medicine, Chengdu, 611137, China.
An innovative colorimetric sensing strategy was developed for the detection of glucose by the integration of glucose aptamer, glucose oxidase (GOx), and horseradish peroxidase (HRP), termed aptamer proximal enzyme cascade reactions (APECR). In the presence of glucose, aptamer binding enables GOx to catalyze glucose oxidation into HO efficiently. Subsequently, the adjacent HRP catalyzes the oxidation of the peroxidase substrate, 2,2'-biazobis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS), utilizing the generated HO, resulting in a distinct color change.
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