Academic literature on the topic 'Oxene-transfer'

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Journal articles on the topic "Oxene-transfer"

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Murugesan, Natesan, and Sidney M. Hecht. "Bleomycin as an oxene transferase. Catalytic oxygen transfer to olefins." Journal of the American Chemical Society 107, no. 2 (1985): 493–500. http://dx.doi.org/10.1021/ja00288a037.

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Kariyawasam, Kalani, Rémy Ricoux, and Jean-Pierre Mahy. "Recent advances in the field of artificial hemoproteins: New efficient eco-compatible biocatalysts for nitrene-, oxene- and carbene-transfer reactions." Journal of Porphyrins and Phthalocyanines 23, no. 11n12 (2019): 1273–85. http://dx.doi.org/10.1142/s1088424619300222.

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In the last few years, the field of artificial hemoproteins has been expanding through two main strategies involving either the incorporation of synthetic metalloporphyrin derivatives into the chiral cavity of a protein or the directed evolution of natural hemoproteins such as myoglobin and cytochromes P450. First, various synthetic water-soluble porphyrins including ions of transition metals such as iron and manganese have been inserted covalently or by supramolecular anchoring into non-specifically designed native proteins or into proteins modified by a minimum number of mutations. The obtai
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Yuan, Lung-Chi, and Thomas C. Bruice. "Use of an oxaziridine as an oxene transfer agent to manganese(III)tetraphenylporphyrin chloride." Journal of the Chemical Society, Chemical Communications, no. 13 (1985): 868. http://dx.doi.org/10.1039/c39850000868.

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Catalano, Carlos E., and Paul R. Ortiz de Montellano. "Oxene transfer, electron abstraction, and cooxidation in the epoxidation of stilbene and 7,8-dihydroxy-7,8-dihydrobenzo[a]pyrene by hemoglobin." Biochemistry 26, no. 25 (1987): 8373–80. http://dx.doi.org/10.1021/bi00399a052.

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Tung, Hui Chan, Pipat Chooto, and Donald T. Sawyer. "Electron-transfer thermodynamics, valence-electron hybridization, and bonding of the meso-tetrakis(2,6-dichlorophenyl)porphinato complexes of manganese, iron, cobalt, nickel, copper, silver, and zinc and of the P+Mn(O) and .bul.P+Fe(O) oxene adducts." Langmuir 7, no. 8 (1991): 1635–41. http://dx.doi.org/10.1021/la00056a015.

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Liu, Zhennan, Yee-Song Law, Ravi Kumar Verma, et al. "A Mn(salen)‐Based Artificial Metalloenzyme for Nitrene and Oxene Transfer Catalysis." ChemBioChem, December 12, 2024. https://doi.org/10.1002/cbic.202400774.

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The development of artificial metalloenzymes (ArMs) offers a potent approach to incorporate non‐natural chemical reactions into biocatalysis. Here we report the assembly of Mn(salen)‐based ArMs by embedding biotinylated Mn(salen) complexes into streptavidin (Sav) variants. Using commercially available nitrene and oxo transfer reagents, these biohybrid catalysts catalyzed the aziridination of alkenes and oxidation of benzylic C‐H bonds with up to 19 and 146 turnover numbers.
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MURUGESAN, N., and S. M. HECHT. "ChemInform Abstract: BLEOMYCIN AS AN OXENE TRANSFERASE. CATALYTIC OXYGEN TRANSFER TO OLEFINS." Chemischer Informationsdienst 16, no. 21 (1985). http://dx.doi.org/10.1002/chin.198521114.

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"Cytochrome P 450 : substrate and prosthetic-group free radicals generated during the enzymatic cycle." Philosophical Transactions of the Royal Society of London. B, Biological Sciences 311, no. 1152 (1985): 579–91. http://dx.doi.org/10.1098/rstb.1985.0165.

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During the enzymatic cycle of the cytochromes P 450 , dioxygen binds to the ferrous haemprotein when the resting ferric haemprotein has undergone a one-electron oxidation after substrate binding. A further one-electron reduction generates an intermediate that is isoelectronic with a peroxide dianion coordinated to a ferric iron. Heterolytic cleavage of the O—O bond generates water and a species which is formally an oxene (oxygen atom) coordinated by iron (III). However, on the basis of model reactions and by analogy to the catalases and peroxidases, this active oxidizing intermediate is formul
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Dissertations / Theses on the topic "Oxene-transfer"

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Kariyawasam, Bowithanthri Kalani. "Nouvelles métalloenzymes artificielles obtenues par couplage covalent de complexes métalliques dans une protéine naturelle (Xylanase A) et dans des protéines artificielles (αReps) Functionalized Artificial Bidomain Proteins Based on an α‑Solenoid Protein Repeat Scaffold: A New Class of Artificial Diels−Alderases Recent advances in the field of artificial hemoproteins: New efficient eco-compatible biocatalysts for nitrene-, oxene- and carbene-transfer reactions Artificial iron hydrogenase made by covalent grafting of Knölker’s complex into xylanase: Application in asymmetric hydrogenation of an aryl ketone in water A new artificial hemoprotein with inducible peroxidase- and monooxygenase-like activities". Thesis, Université Paris-Saclay (ComUE), 2019. http://www.theses.fr/2019SACLS518.

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Dans un contexte de développement durable, les enzymes sont des outils biologiques puissants pour catalyser des réactions avec de très grandes efficacités et spécificités. Inspirée des enzymes et de la catalyse organométallique, l’élaboration de métalloenzymes artificielles émerge depuis plusieurs années comme une stratégie de choix pour fournir aux chimistes de nouveaux biocatalyseurs, en accord avec les principes de la chimie verte. Elles sont construites par l’insertion par interactions supramoléculaires ou couplage covalent, d’un ion ou d’un complexe métallique au sein d’une protéine, qui
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