Results 1 to 10 of about 23,484 (216)
Artificial Metalloenzymes [PDF]
ChemCatChem, 2010 Artificial metalloenzymes have emerged as a promising approach to merge the attractive properties of homogeneous catalysis and biocatalysis. The activity and selectivity, including enantioselectivity, of natural metalloenzymes are due to the second coordination sphere interactions provided by the protein.
Rosati, Fiora, Roelfes, Gerard
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Heme Oxygenase-Like Metalloenzymes. [PDF]
Annu Rev BiochemHeme oxygenase (HO)-like metalloenzymes are an emerging protein superfamily diverse in reaction outcome and mechanism. Found primarily in bacterial biosynthetic pathways, members conserve a flexible protein scaffold shared with the heme catabolic enzyme, HO, and a set of metal-binding residues.
Pope SR +6 more
europepmc +4 more sources
Targeting Metalloenzymes: The “Achilles’ Heel” of Viruses and Parasites
Pharmaceuticals, 2023 Metalloenzymes are central to the regulation of a wide range of essential viral and parasitic functions, including protein degradation, nucleic acid modification, and many others.
Dimitrios Moianos +3 more
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Molecules, 2021 A series of benzenesulfonamides incorporating pyrazole- and pyridazinecarboxamides decorated with several bulky moieties has been obtained by original procedures.
Andrea Angeli +8 more
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Machine Learning Approaches for Metalloproteins
Molecules, 2022 Metalloproteins are a family of proteins characterized by metal ion binding, whereby the presence of these ions confers key catalytic and ligand-binding properties.
Yue Yu, Ruobing Wang, Ruijie D. Teo
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Evaluation of Metallo-β-Lactamase Susceptibility Testing in a Physiologic Medium
Microbiology Spectrum, 2021 Research in identifying alternative growth media that better mimic host conditions is gaining ground. Relative to nutrient-rich Mueller-Hinton broth (MHB), data on the influence of physiologic or host-mimicking media on metallo-β-lactamase (MBL ...
Tomefa E. Asempa +4 more
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Nitrogenase beyond the Resting State: A Structural Perspective
Molecules, 2023 Nitrogenases have the remarkable ability to catalyze the reduction of dinitrogen to ammonia under physiological conditions. How does this happen? The current view of the nitrogenase mechanism focuses on the role of hydrides, the binding of dinitrogen in ...
Rebeccah A. Warmack, Douglas C. Rees
doaj +1 more source
Selective targeting of proteins by hybrid polyoxometalates: Interaction between a bis-biotinylated hybrid conjugate and avidin [PDF]
, 2018 The Keggin-type polyoxometalate [\u3b3-SiW10O36]8 12 was covalently modified to obtain a bis-biotinylated conjugate able to bind avidin. Spectroscopic studies such as UV-vis, fluorimetry, circular dichroism, coupled to surface plasmon resonance technique
Alessandra Saccani +12 more
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Current Medicinal Chemistry, 2019 Epigenetics controls the expression of genes and is responsible for cellular phenotypes. The fundamental basis of these mechanisms involves in part the post-translational modifications (PTMs) of DNA and proteins, in particular, the nuclear histones. DNA can be methylated or demethylated on cytosine.
Blanquart, Christophe +5 more
openaire +5 more sources
The Geometry of the Catalytic Active Site in [FeFe]-hydrogenases is Determined by Hydrogen Bonding and Proton Transfer [PDF]
, 2019 [FeFe]-hydrogenases are efficient metalloenzymes that catalyze the oxidation and evolution of molecular hydrogen, H2. They serve as a blueprint for the design of synthetic H2-forming catalysts.
Apfel, Ulf-Peter +11 more
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