Works about COFACTORS (Biochemistry)
Results: 830
Bacteria at Work – Experimental and Theoretical Studies Reveal the Catalytic Mechanism of Ectoine Synthase.
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- Chemistry - A European Journal, 2024, v. 30, n. 23, p. 1, doi. 10.1002/chem.202304163
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Synthesis of 3‐Phenylserine by a Two‐enzyme Cascade System with PLP Cofactor.
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- Chemistry - A European Journal, 2024, v. 30, n. 10, p. 1, doi. 10.1002/chem.202302959
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Stable and Reusable Fe<sub>3</sub>O<sub>4</sub>/ZIF‐8 Composite for Encapsulation of FDH Enzyme under Mild Conditions Applicable to CO<sub>2</sub> Reduction.
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- Chemistry - A European Journal, 2023, v. 29, n. 47, p. 1, doi. 10.1002/chem.202301113
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Activity Sensing of Coagulation and Fibrinolytic Proteases.
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- Chemistry - A European Journal, 2023, v. 29, n. 18, p. 1, doi. 10.1002/chem.202203473
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Current State of [Fe]‐Hydrogenase and Its Biomimetic Models.
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- Chemistry - A European Journal, 2022, v. 28, n. 57, p. 1, doi. 10.1002/chem.202201499
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Properties of the Reactants and Their Interactions within and with the Enzyme Binding Cavity Determine Reaction Selectivities. The Case of Fe(II)/2‐Oxoglutarate Dependent Enzymes.
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- Chemistry - A European Journal, 2022, v. 28, n. 18, p. 1, doi. 10.1002/chem.202104106
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Secondary Amine Catalysis in Enzyme Design: Broadening Protein Template Diversity through Genetic Code Expansion.
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- Angewandte Chemie, 2024, v. 136, n. 22, p. 1, doi. 10.1002/ange.202403098
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Enhancing Flavins Photochemical Activity in Hydrogen Atom Abstraction and Triplet Sensitization through Ring‐Contraction.
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- Angewandte Chemie, 2024, v. 136, n. 16, p. 1, doi. 10.1002/ange.202318590
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Flavin‐N5OOH Functions as both a Powerful Nucleophile and a Base in the Superfamily of Flavoenzymes.
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- Angewandte Chemie, 2024, v. 136, n. 14, p. 1, doi. 10.1002/ange.202318629
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Harmonizing Enzyme‐like Cofactors to Boost Nanozyme Catalysis.
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- Angewandte Chemie, 2024, v. 136, n. 11, p. 1, doi. 10.1002/ange.202319108
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Acyl and CO Ligands in the [Fe]‐Hydrogenase Cofactor Scramble upon Photolysis.
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- Angewandte Chemie, 2024, v. 136, n. 6, p. 1, doi. 10.1002/ange.202316478
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Non‐native Intramolecular Radical Cyclization Catalyzed by a B<sub>12</sub>‐Dependent Enzyme.
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- Angewandte Chemie, 2023, v. 135, n. 51, p. 1, doi. 10.1002/ange.202312893
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Manganese Transfer Hydrogenases Based on the Biotin‐Streptavidin Technology.
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- Angewandte Chemie, 2023, v. 135, n. 43, p. 1, doi. 10.1002/ange.202311896
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Co‐encapsulating Cofactor and Enzymes in Hydrogen‐Bonded Organic Frameworks for Multienzyme Cascade Reactions with Cofactor Recycling.
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- Angewandte Chemie, 2023, v. 135, n. 42, p. 1, doi. 10.1002/ange.202308562
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Polyketide Synthase‐Mediated O‐Methyloxime Formation in the Biosynthesis of the Oximidine Anticancer Agents.
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- Angewandte Chemie, 2023, v. 135, n. 34, p. 1, doi. 10.1002/ange.202304476
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Selecting Better Biocatalysts by Complementing Recoded Bacteria.
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- Angewandte Chemie, 2023, v. 135, n. 2, p. 1, doi. 10.1002/ange.202213942
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The Function of Two Radical‐SAM Enzymes, HcgA and HcgG, in the Biosynthesis of the [Fe]‐Hydrogenase Cofactor.
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- Angewandte Chemie, 2022, v. 134, n. 50, p. 1, doi. 10.1002/ange.202213239
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[FeFe]‐Hydrogenase In Vitro Maturation.
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- Angewandte Chemie, 2022, v. 134, n. 49, p. 1, doi. 10.1002/ange.202212074
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Co‐compartmentalization of Enzymes and Cofactors within Pickering Emulsion Droplets for Continuous‐Flow Catalysis.
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- Angewandte Chemie, 2022, v. 134, n. 45, p. 1, doi. 10.1002/ange.202211912
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An Fe<sub>6</sub>C Core in All Nitrogenase Cofactors.
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- Angewandte Chemie, 2022, v. 134, n. 41, p. 1, doi. 10.1002/ange.202209190
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Structure‐Based Demystification of Radical Catalysis by a Coenzyme B<sub>12</sub> Dependent Enzyme—Crystallographic Study of Glutamate Mutase with Cofactor Homologues.
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- Angewandte Chemie, 2022, v. 134, n. 35, p. 1, doi. 10.1002/ange.202208295
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A Cobalamin‐Dependent Radical SAM Enzyme Catalyzes the Unique C<sub>α</sub>‐Methylation of Glutamine in Methyl‐Coenzyme M Reductase.
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- Angewandte Chemie, 2022, v. 134, n. 32, p. 1, doi. 10.1002/ange.202204198
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A Pair of Atypical KAS III Homologues with Initiation and Elongation Functions Program the Polyketide Biosynthesis in Asukamycin.
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- Angewandte Chemie, 2022, v. 134, n. 19, p. 1, doi. 10.1002/ange.202200879
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Synthesis of Enantiopure Sulfoxides by Concurrent Photocatalytic Oxidation and Biocatalytic Reduction.
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- Angewandte Chemie, 2022, v. 134, n. 17, p. 1, doi. 10.1002/ange.202117103
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Structural Insight into the Catalytic Mechanism of the Endoperoxide Synthase FtmOx1.
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- Angewandte Chemie, 2022, v. 134, n. 12, p. 1, doi. 10.1002/ange.202112063
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Emergence of a Promiscuous Peroxidase Under Non‐Equilibrium Conditions**.
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- Angewandte Chemie, 2022, v. 134, n. 2, p. 1, doi. 10.1002/ange.202111857
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Unexpected Reactions of α,β‐Unsaturated Fatty Acids Provide Insight into the Mechanisms of CYP152 Peroxygenases.
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- Angewandte Chemie, 2021, v. 133, n. 46, p. 24899, doi. 10.1002/ange.202111163
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Engineering Dirhodium Artificial Metalloenzymes for Diazo Coupling Cascade Reactions**.
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- Angewandte Chemie, 2021, v. 133, n. 44, p. 23865, doi. 10.1002/ange.202107982
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Surprising Condensation Reactions of the Azadithiolate Cofactor.
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- Angewandte Chemie, 2021, v. 133, n. 38, p. 20912, doi. 10.1002/ange.202108135
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Influence of Magnetic Fields on Electrochemical Reactions of Redox Cofactor Solutions.
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- Angewandte Chemie, 2021, v. 133, n. 33, p. 18443, doi. 10.1002/ange.202106288
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Controlled Ligand Exchange Between Ruthenium Organometallic Cofactor Precursors and a Naïve Protein Scaffold Generates Artificial Metalloenzymes Catalysing Transfer Hydrogenation.
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- Angewandte Chemie, 2021, v. 133, n. 19, p. 11014, doi. 10.1002/ange.202015834
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Structural Characterization of Two CO Molecules Bound to the Nitrogenase Active Site.
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- Angewandte Chemie, 2021, v. 133, n. 11, p. 5768, doi. 10.1002/ange.202015751
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In Vivo Assembly of Artificial Metalloenzymes and Application in Whole‐Cell Biocatalysis*.
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- Angewandte Chemie, 2021, v. 133, n. 11, p. 5978, doi. 10.1002/ange.202014771
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Hierarchically Porous Biocatalytic MOF Microreactor as a Versatile Platform towards Enhanced Multienzyme and Cofactor‐Dependent Biocatalysis.
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- Angewandte Chemie, 2021, v. 133, n. 10, p. 5481, doi. 10.1002/ange.202014002
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Making or Breaking Metal‐Dependent Catalytic Activity: The Role of Stammers in Designed Three‐Stranded Coiled Coils.
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- Angewandte Chemie, 2020, v. 132, n. 46, p. 20625, doi. 10.1002/ange.202008356
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Refactoring the Concise Biosynthetic Pathway of Cyanogramide Unveils Spirooxindole Formation Catalyzed by a P450 Enzyme.
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- Angewandte Chemie, 2020, v. 132, n. 33, p. 14169, doi. 10.1002/ange.202004978
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Discovery of a Dual Function Cytochrome P450 that Catalyzes Enyne Formation in Cyclohexanoid Terpenoid Biosynthesis.
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- Angewandte Chemie, 2020, v. 132, n. 32, p. 13639, doi. 10.1002/ange.202004435
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Exploiting Cofactor Versatility to Convert a FAD‐Dependent Baeyer–Villiger Monooxygenase into a Ketoreductase.
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- Angewandte Chemie, 2019, v. 131, n. 41, p. 14641, doi. 10.1002/ange.201907606
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Spectroscopic Characterization of an Eight‐Iron Nitrogenase Cofactor Precursor that Lacks the "9<sup>th</sup> Sulfur".
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- Angewandte Chemie, 2019, v. 131, n. 41, p. 14845, doi. 10.1002/ange.201907593
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Cofactor Controlled Encapsulation of a Rhodium Hydroformylation Catalyst.
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- Angewandte Chemie, 2019, v. 131, n. 9, p. 2722, doi. 10.1002/ange.201812610
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Golgi in copper homeostasis: a view from the membrane trafficking field.
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- Histochemistry & Cell Biology, 2013, v. 140, n. 3, p. 285, doi. 10.1007/s00418-013-1123-8
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Cofactor-embedded nanoporous activated carbon matrices for the immobilization of intracellular enzymes and degradation of endocrine disruptor.
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- Biotechnology & Applied Biochemistry, 2017, v. 64, n. 3, p. 364, doi. 10.1002/bab.1492
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Enhancement of NAD(H) pool for formation of oxidized biochemicals in Escherichia coli.
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- Journal of Industrial Microbiology & Biotechnology, 2018, v. 45, n. 11, p. 939, doi. 10.1007/s10295-018-2072-y
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Redox cofactor engineering in industrial microorganisms: strategies, recent applications and future directions.
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- Journal of Industrial Microbiology & Biotechnology, 2018, v. 45, n. 5, p. 313, doi. 10.1007/s10295-018-2031-7
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Engineering cofactor flexibility enhanced 2,3-butanediol production in Escherichia coli.
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- Journal of Industrial Microbiology & Biotechnology, 2017, v. 44, n. 12, p. 1605, doi. 10.1007/s10295-017-1986-0
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Construction and evaluation of a novel bifunctional phenylalanine-formate dehydrogenase fusion protein for bienzyme system with cofactor regeneration.
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- Journal of Industrial Microbiology & Biotechnology, 2016, v. 43, n. 5, p. 577, doi. 10.1007/s10295-016-1738-6
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The many roles of glutamate in metabolism.
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- Journal of Industrial Microbiology & Biotechnology, 2016, v. 43, n. 2/3, p. 419, doi. 10.1007/s10295-015-1665-y
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Construction of allitol synthesis pathway by multi-enzyme coexpression in Escherichia coli and its application in allitol production.
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- Journal of Industrial Microbiology & Biotechnology, 2015, v. 42, n. 5, p. 661, doi. 10.1007/s10295-014-1578-1
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Redirecting metabolic flux in Saccharomyces cerevisiae through regulation of cofactors in UMP production.
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- Journal of Industrial Microbiology & Biotechnology, 2015, v. 42, n. 4, p. 577, doi. 10.1007/s10295-014-1536-y
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Metabolic engineering of carbon and redox flow in the production of small organic acids.
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- Journal of Industrial Microbiology & Biotechnology, 2015, v. 42, n. 3, p. 403, doi. 10.1007/s10295-014-1560-y
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