569-77-7Relevant articles and documents
Enhanced Activity of Enzymes Encapsulated in Hydrophilic Metal-Organic Frameworks
Liang, Weibin,Xu, Huoshu,Carraro, Francesco,Maddigan, Natasha K.,Li, Qiaowei,Bell, Stephen G.,Huang, David M.,Tarzia, Andrew,Solomon, Marcello B.,Amenitsch, Heinz,Vaccari, Lisa,Sumby, Christopher J.,Falcaro, Paolo,Doonan, Christian J.
, (2019)
Encapsulation of biomacromolecules in metal-organic frameworks (MOFs) can preserve biological functionality in harsh environments. Despite the success of this approach, termed biomimietic mineralization, limited consideration has been given to the chemistry of the MOF coating. Here, we show that enzymes encapsulated within hydrophilic MAF-7 or ZIF-90 retain enzymatic activity upon encapsulation and when exposed to high temperatures, denaturing or proteolytic agents, and organic solvents, whereas hydrophobic ZIF-8 affords inactive catalase and negligible protection to urease.
Post-synthetic transformation of a Zn(II) polyhedral coordination network into a new supramolecular isomer of HKUST-1
Chen, Yao,Wojtas, Lukasz,Ma, Shengqian,Zaworotko, Michael J.,Zhang, Zhenjie
, p. 8866 - 8869 (2017)
A Zn-based porphyrin containing metal-organic material (porphMOM-1) was transformed into a novel Cu-based porphyrin-encapsulating metal-organic material (porph@HKUST-1-β) via a one-pot post-synthetic modification (PSM) process involving both metal ion exchange and linker installation of trimesic acid. HKUST-1-β is the first example of yao topology and is to our knowledge the first supramolecular isomer of the archetypal coordination network HKUST-1.
A low molecular weight hydrogel which exhibits electroosmotic flow and its use as a bioreactor and for electrochromatography of neutral species
Mizrahi, Shaul,Rizkov, Dan,Hayat, Netanel,Lev, Ovadia
, p. 2914 - 2916 (2008)
A low molecular weight hydrogel which exhibits electroosmotic flow is described, and its use for separation and biocatalytic applications that require passage of a solvent stream through the gel is demonstrated. The Royal Society of Chemistry.
Mimicking peroxidase activity by a polymer-supported oxidovanadium(IV) Schiff base complex derived from salicylaldehyde and 1,3-diamino-2-hydroxypropane
Maurya, Mannar R.,Chaudhary, Nikita,Avecilla, Fernando,Correia, Isabel
, p. 181 - 192 (2015)
The polymer-supported oxidovanadium(IV) complex PS-[VIVO(sal-dahp)] (2) (PS = chloromethylated polystyrene crosslinked with 5% divinylbenzene, and H3sal-dahp = dibasic pentadentate ligand derived from salicylaldehyde and 1,3-diamino-2-hydroxypropane) was prepared from the corresponding monomeric oxidovanadium(IV) complex [VIVO(Hsal-dahp)(DMSO)] (1), characterized and successfully used as catalyst for the peroxidase-like oxidation of pyrogallol. The oxidation of pyrogallol to purpurogallin with PS-[VIVO(sal-dahp)] (2) was achieved under mild conditions at pH 7 buffered solution. Plausible intermediate species formed during peroxidase mimicking experiments are proposed, by studying the model complex [VIVO(Hsal-dahp)(DMSO)] (1) by UV-visible and 51V NMR spectroscopies. The high peroxidase mimicking ability of polymer-supported complex 2, its stability in a wide pH range, the easy separation from the reaction media, and the reusability without considerable decrease in activity, suggest that this heterogeneous catalyst has high potential for application in sustainable industrial catalysis.
Oxidation of ethanol induced by simple polyphenols: Prooxidant property of polyphenols
Inui, Takako,Nakahara, Koichi,Uchida, Masaaki,Miki, Wataru,Unoura, Kei,Kokeguchi, Yuki,Hosokawa, Takahiro
, p. 1201 - 1207 (2004)
The aerobic oxidation of ethanol to acetaldehyde in water is induced by simple polyphenols, such as pyrogallol or catechol, in the presence of FeSO 4-DTPA (N,N,N′,N′′,N′′- diethylenetriaminepentaacetic acid) catalyst. The amount of acetaldehyde formed becomes an indicator of their "prooxidant" ability in terms of the activation of O2. The "prooxidant" ability of pyrogallol is higher than that of catechol. Electron-withdrawing substituents decrease the ability, whereas electron-donating ones enhance it. The "prooxidant" property is exhibited by the total consequence of two processes: hydroxyl radical (OH) generation from O2 and its capture by phenolic compounds.
Peroxidase activity of cationic metalloporphyrin-antibody complexes
Yamaguchi, Hiroyasu,Tsubouchi, Kaori,Kawaguchi, Kazuhide,Horita, Eri,Harada, Akira
, p. 6179 - 6186 (2004)
Peroxidase activity of a complex of water-soluble cationic metalloporphyrin with anti-cationic porphyrin antibody is reported. Antibody 12E11G, which was prepared by immunization with a conjugate of 5-(4-carboxyphenyl)-10,15,20- tris(4-methylpyridyl)porphine iodide (3MPy1C), bound to tetramethylpyridylporphyrin iron complex (FeIII-TMPyP) with the dissociation constant of 2.6 × 10-7M. The complex of antibody 12E11G with FeIII-TMPyP catalyzed oxidation of pyrogallol, catechol, and guaiacol. A Lineweaver-Burk plot for the oxidation of pyrogallol catalyzed by the FeIII-TMPyP-antibody complex showed Km = 8.6mM and kcat = 680 min-1. Under the same conditions, K m, and Kcat for horseradish peroxidase (HRP) were 0.8 mM and 1750 min-1, respectively. Although the binding interaction of the antibody to the substrates was one order lower than that of native HRP, the peroxidase activity of this system was in the same order of magnitude as that of HRP.
Biomimetic catalysis of a porous iron-based metal-metalloporphyrin framework
Chen, Yao,Hoang, Tran,Ma, Shengqian
, p. 12600 - 12602 (2012)
A porous metal-metalloporphyrin framework, MMPF-6, based upon an iron(III)-metalated porphyrin ligand and a secondary binding unit of a zirconium oxide cluster was constructed; MMPF-6 demonstrated interesting peroxidase activity comparable to that of the heme protein myoglobin as well as exhibited solvent adaptability of retaining the peroxidase activity in an organic solvent.
A graphene oxide/hemoglobin composite hydrogel for enzymatic catalysis in organic solvents
Huang, Cancan,Bai, Hua,Li, Chun,Shi, Gaoquan
, p. 4962 - 4964 (2011)
A graphene oxide/hemoglobin (GO/Hb) composite hydrogel was prepared for catalyzing a peroxidatic reaction in organic solvents with high yields, exceptional activity and stability.
Synthesis of reduced graphene oxide-iron nanoparticles with superior enzyme-mimetic activity for biosensing application
Li, Lili,Zeng, Chunmei,Ai, Lunhong,Jiang, Jing
, p. 470 - 477 (2015)
Development of enzyme-mimetic catalysts with sustainability and environmental benignancy has gained considerable attention with the growing demands for large-scale applications in recent years. Here, we demonstrate that the reduced graphene oxide (RGO)-iron nanoparticles (INs) can be utilized as the highly active and cost-effective enzyme-mimetic catalysts for the first time, which have been successfully synthesized by a facile iron-self-catalysis process at room temperature. Benefitting from synergetic effects between RGO and INs, the RGO-INs could efficiently catalyze the oxidization of 3,3′,5,5′-tetramethylbenzidine (TMB) in the presence of H2O2 to produce a typical color reaction, showing the much better peroxidase-like activity than that of each individual part. The mechanistic insight into the enhanced peroxidase-like activity of the RGO-INs was investigated systematically. On the basis of the enzyme-mimetic activity of the RGO-INs, the simple, sensitive, selective and cost-effective colorimetric assays for the detection of hydrogen peroxide and glucose with naked eyes were successfully established. The RGO-INs showed several prominent advantages, such as facile preparation, low cost, tunability in catalytic activity, and low detection limit, over natural peroxidase or other nanomaterial-based alternatives, holding great potential as enzymatic mimics for biosensing applications.
Dioxidomolybdenum(VI) Complexes of Tripodal Tetradentate Ligands for Catalytic Oxygen Atom Transfer between Benzoin and Dimethyl Sulfoxide and for Oxidation of Pyrogallol
Maurya, Mannar R.,Uprety, Bhawna,Avecilla, Fernando
, p. 4802 - 4813 (2016)
The reactions of the tripodal tetradentate ONNO donor ligands 6,6′-{[(2-morpholinoethyl)azanediyl]bis(methylene)}bis(2,4-di-tert-butylphenol) (H2L1), 6,6′-{[(2-morpholinoethyl)azanediyl]bis(methylene)}bis(2,4-dimethylphenol) (H2L2) and 6,6′-{[(2-morpholinoethyl)azanediyl]bis(methylene)}bis[2-(tert-butyl)-4-methylphenol] (H2L3) with [MoVIO2(acac)2] (acac = acetylacetonato) in a 1:1 molar ratio in MeOH gave the corresponding cis-dioxidomolybdenum(VI) complexes [MoO2(L1)], [MoO2(L2)] and [MoO2(L3)], respectively, in excellent yields. These complexes were characterized by various spectroscopic (IR, UV/Vis,1H and13C NMR), electrochemical, thermogravimetric, single-crystal XRD, and powder XRD (PXRD) studies. In these complexes, the geometry around the cis-[MoO2]2+core is distorted octahedral, and the ligands are tetradentate and coordinate through two Ophenolate, one Ntripodal, and one Nmorpholineatoms. One of the oxido groups and the morpholine nitrogen atom occupy the axial sites. These complexes were used for catalytic oxygen atom transfer between benzoin and dimethyl sulfoxide (DMSO) in acetonitrile at 80 °C, and the formation of benzil was followed by HPLC. Detailed kinetic studies revealed a first-order rate in benzoin and catalyst, and the rate constant for the second-order oxygen atom transfer reaction was 0.0162 m–1h–1. The formation of the dinuclear intermediates [LMoV–μ-O-MoVL] was established by MALDI-TOF MS and UV/Vis spectroscopy. Its reversible nature was further supplemented by UV/Vis spectroscopy. These complexes also catalyze the oxidation of pyrogallol in a fashion similar to that of transhydroxylases. Under aerobic conditions, the initially formed oxidation product phloroglucinol undergoes further oxidative coupling in the presence of H2O2to give purpurogallin as the final product. This process follows Michaelis–Menten-type kinetics with respect to pyrogallol; the kcatvalues obtained were 394, 300 and 247 h–1for [MoVIO2(L1)], [MoVIO2(L2)] and [MoVIO2(L3)], respectively.
