Structure refinement of the aldehyde oxidoreductase from Desulfovibrio gigas (MOP) at 1.28 A
about
High resolution crystal structures of the wild type and Cys-55-->Ser and Cys-59-->Ser variants of the thioredoxin-like [2Fe-2S] ferredoxin from Aquifex aeolicusThe First Mammalian Aldehyde Oxidase Crystal Structure: INSIGHTS INTO SUBSTRATE SPECIFICITYKinetic and Structural Studies of Aldehyde Oxidoreductase from Desulfovibrio gigas Reveal a Dithiolene-Based Chemistry for Enzyme Activation and Inhibition by H2O2Aromatic aldehydes at the active site of aldehyde oxidoreductase from Desulfovibrio gigas: reactivity and molecular details of the enzyme-substrate and enzyme-product interactionDOM-fold: a structure with crossing loops found in DmpA, ornithine acetyltransferase, and molybdenum cofactor-binding domainGene cluster of Arthrobacter ilicis Ru61a involved in the degradation of quinaldine to anthranilate: characterization and functional expression of the quinaldine 4-oxidase qoxLMS genes.Investigation of metal-dithiolate fold angle effects: implications for molybdenum and tungsten enzymes.Mammalian molybdo-flavoenzymes, an expanding family of proteins: structure, genetics, regulation, function and pathophysiology.Metal-sulfur valence orbital interaction energies in metal-dithiolene complexes: determination of charge and overlap interaction energies by comparison of core and valence ionization energy shifts.Archaeal Mo-Containing Glyceraldehyde Oxidoreductase Isozymes Exhibit Diverse Substrate Specificities through Unique Subunit Assemblies.Photoelectron spectroscopy and electronic structure calculations of d1 vanadocene compounds with chelated dithiolate ligands: implications for pyranopterin Mo/W enzymes.Metalloproteins containing cytochrome, iron-sulfur, or copper redox centersShifting the metallocentric molybdoenzyme paradigm: the importance of pyranopterin coordination.Electronic structure contributions to reactivity in xanthine oxidase family enzymes.Nitrite reduction by molybdoenzymes: a new class of nitric oxide-forming nitrite reductases.Predicting Protein-Protein Interactions Using BiGGER: Case Studies.Pyranopterin Coordination Controls Molybdenum Electrochemistry in Escherichia coli Nitrate Reductase.On the purification and preliminary crystallographic analysis of isoquinoline 1-oxidoreductase from Brevundimonas diminuta 7Reductive half-reaction of aldehyde oxidoreductase toward acetaldehyde: Ab initio and free energy quantum mechanical/molecular mechanical calculations.Functional expression of the quinoline 2-oxidoreductase genes (qorMSL) in Pseudomonas putida KT2440 pUF1 and in P. putida 86-1 deltaqor pUF1 and analysis of the Qor proteins.Structural and biochemical identification of a novel bacterial oxidoreductase.
P2860
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P2860
Structure refinement of the aldehyde oxidoreductase from Desulfovibrio gigas (MOP) at 1.28 A
description
2001 nî lūn-bûn
@nan
2001 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Structure refinement of the al ...... fovibrio gigas (MOP) at 1.28 A
@ast
Structure refinement of the al ...... fovibrio gigas (MOP) at 1.28 A
@en
Structure refinement of the al ...... fovibrio gigas (MOP) at 1.28 A
@nl
type
label
Structure refinement of the al ...... fovibrio gigas (MOP) at 1.28 A
@ast
Structure refinement of the al ...... fovibrio gigas (MOP) at 1.28 A
@en
Structure refinement of the al ...... fovibrio gigas (MOP) at 1.28 A
@nl
prefLabel
Structure refinement of the al ...... fovibrio gigas (MOP) at 1.28 A
@ast
Structure refinement of the al ...... fovibrio gigas (MOP) at 1.28 A
@en
Structure refinement of the al ...... fovibrio gigas (MOP) at 1.28 A
@nl
P2093
P356
P1476
Structure refinement of the al ...... fovibrio gigas (MOP) at 1.28 A
@en
P2093
P2888
P304
P356
10.1007/S007750100255
P577
2001-10-01T00:00:00Z
P5875
P6179
1044882777