Results 11 to 20 of about 11,336 (207)
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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The NOX Family of Proteins Is Also Present in Bacteria
mBio, 2017 Transmembrane NADPH oxidase (NOX) enzymes have been so far only characterized in eukaryotes. In most of these organisms, they reduce molecular oxygen to superoxide and, depending on the presence of additional domains, are called NOX or dual oxidases ...
Christine Hajjar +7 more
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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
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Nickel-dependent metalloenzymes [PDF]
Archives of Biochemistry and Biophysics, 2014 This review describes the functions, structures, and mechanisms of nine nickel-containing enzymes: glyoxalase I, acireductone dioxygenase, urease, superoxide dismutase, [NiFe]-hydrogenase, carbon monoxide dehydrogenase, acetyl-coenzyme A synthase/decarbonylase, methyl-coenzyme M reductase, and lactate racemase.
Jodi L, Boer +2 more
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Molecules, 2018 We report the cloning and catalytic activity of a β-carbonic anhydrase (CA, EC 4.2.1.1), isolated from the pathogenic protozoan Entamoeba histolytica, EhiCA.
Susanna Haapanen +4 more
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Mysteries of Metals in Metalloenzymes [PDF]
Accounts of Chemical Research, 2014 Natural metalloenzymes are often the most proficient catalysts in terms of their activity, selectivity, and ability to operate at mild conditions. However, metalloenzymes are occasionally surprising in their selection of catalytic metals, and in their responses to metal substitution.
Valdez, Crystal E +3 more
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Angewandte Chemie, EarlyView.Directional control within the secondary coordination sphere redefines CO2 reduction by iron porphyrins. Simply rearranging identical urea hydrogen‐bond donors modulates reactivity, revealing that optimal catalysis does not only arise from maximal intermediate stabilization, but also from directional, adaptive non‐covalent interactions that balance ...
Ashutosh Vishwakarma +7 more
wiley +2 more sources
Amino Acids as Building Blocks for Carbonic Anhydrase Inhibitors
Metabolites, 2018 Carbonic anhydrases (CAs) are a superfamily of metalloenzymes widespread in all life, classified into seven genetically different families (α–θ).
Niccolò Chiaramonte +3 more
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