Pyranopterin conformation defines the function of molybdenum and tungsten enzymes. - Wikidata - wikimedia - TriplyDB

Pyranopterin conformation defines the function of molybdenum and tungsten enzymes.

Pyranopterin conformation defines the function of molybdenum and tungsten enzymes.

http://www.wikidata.org/entity/Q36236182

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Kinetic and Structural Studies of Aldehyde Oxidoreductase from Desulfovibrio gigas Reveal a Dithiolene-Based Chemistry for Enzyme Activation and Inhibition by H2O2 Structural basis of thermal stability of the tungsten cofactor synthesis protein MoaB from Pyrococcus furiosus Nitrate and periplasmic nitrate reductases Sulfur K-edge X-ray absorption spectroscopy and density functional theory calculations on monooxo Mo(IV) and bisoxo Mo(VI) bis-dithiolenes: insights into the mechanism of oxo transfer in sulfite oxidase and its relation to the mechanism of DMSO redu The mononuclear molybdenum enzymes.Pyranopterin dithiolene distortions relevant to electron transfer in xanthine oxidase/dehydrogenase.Recent developments in the study of molybdoenzyme models.Archaeal Mo-Containing Glyceraldehyde Oxidoreductase Isozymes Exhibit Diverse Substrate Specificities through Unique Subunit Assemblies.Electrochemical evidence that pyranopterin redox chemistry controls the catalysis of YedY, a mononuclear Mo enzyme.Large Ligand Folding Distortion in an Oxomolybdenum Donor-Acceptor Complex.YedY: A Mononuclear Molybdenum Enzyme with a Redox-Active Ligand?Molybdenum and tungsten oxygen transferases--and functional diversity within a common active site motif.Shifting the metallocentric molybdoenzyme paradigm: the importance of pyranopterin coordination.Electronic structure contributions to reactivity in xanthine oxidase family enzymes.Solvent-Dependent Pyranopterin Cyclization in Molybdenum Cofactor Model Complexes.Pyranopterin Coordination Controls Molybdenum Electrochemistry in Escherichia coli Nitrate Reductase.Pulsed electron paramagnetic resonance spectroscopy of (33)S-labeled molybdenum cofactor in catalytically active bioengineered sulfite oxidase.Structure and reversible pyran formation in molybdenum pyranopterin dithiolene models of the molybdenum cofactor.QM/MM study of the reaction mechanism of sulfite oxidase.Structural Insights into the Incorporation of the Mo Cofactor into Sulfite Oxidase from Site-Directed Spin Labeling.

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P2860

Pyranopterin conformation defines the function of molybdenum and tungsten enzymes.

http://www.wikidata.org/entity/Q36236182

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Pyranopterin conformation defines the function of molybdenum and tungsten enzymes.

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Pyranopterin conformation defines the function of molybdenum and tungsten enzymes.

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type

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Pyranopterin conformation defines the function of molybdenum and tungsten enzymes.

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Pyranopterin conformation defines the function of molybdenum and tungsten enzymes.

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Pyranopterin conformation defines the function of molybdenum and tungsten enzymes.

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Pyranopterin conformation defines the function of molybdenum and tungsten enzymes.

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PNAS.1200671109

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Pyranopterin conformation defines the function of molybdenum and tungsten enzymes

@en

P2093

Benjamin Stein

http://www.w3.org/2001/XMLSchema#string

Joel H Weiner

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Martin L Kirk

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Matthew Solomonson

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P2860

Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A

The crystal structure of Cupriavidus necator nitrate reductase in oxidized and partially reduced states

Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase

Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions

Molybdenum cofactor biosynthesis and molybdenum enzymes

Evolutionary persistence of the molybdopyranopterin-containing sulfite oxidase protein fold

Molybdenum cofactors, enzymes and pathways.

Molybdenum enzymes containing the pyranopterin cofactor: an overview.

Pterin chemistry and its relationship to the molybdenum cofactor.

Spectroscopic and electronic structure studies of a dimethyl sulfoxide reductase catalytic intermediate: implications for electron- and atom-transfer reactivity

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14773-14778

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10.1073/PNAS.1200671109

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37

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109

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Richard Rothery

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2012-08-27T00:00:00Z

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