Crystal structure of DMSO reductase: redox-linked changes in molybdopterin coordination.
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Cell biology and molecular basis of denitrificationReversible interconversion of carbon dioxide and formate by an electroactive enzymeStructure of the non-redox-active tungsten/[4Fe:4S] enzyme acetylene hydrataseInsights into the respiratory electron transfer pathway from the structure of nitrate reductase AThe 1.38 Å crystal structure of DmsD protein fromSalmonella typhimurium, a proofreading chaperone on the Tat pathwayMolecular mechanism of energy conservation in polysulfide respirationCloning and sequencing of the genes encoding the periplasmic-cytochrome B-containing selenate reductase of Thauera selenatisHeavy metal ions inhibit molybdoenzyme activity by binding to the dithiolene moiety of molybdopterin in Escherichia coliNitrate and periplasmic nitrate reductasesThe DMSO Reductase Family of Microbial Molybdenum Enzymes; Molecular Properties and Role in the Dissimilatory Reduction of Toxic ElementsCrystal structure of pyrogallol-phloroglucinol transhydroxylase, an Mo enzyme capable of intermolecular hydroxyl transfer between phenols.Evolutionary persistence of the molybdopyranopterin-containing sulfite oxidase protein foldThe molybdenum oxotransferases and related enzymes.Structural data on the periplasmic aldehyde oxidoreductase PaoABC from Escherichia coli: SAXS and preliminary X-ray crystallography analysis.Cloning, sequencing and heterologous expression of pyrogallol-phloroglucinol transhydroxylase from Pelobacter acidigallici.Genomic analysis of anaerobic respiration in the archaeon Halobacterium sp. strain NRC-1: dimethyl sulfoxide and trimethylamine N-oxide as terminal electron acceptorsPhysiological and genetic analyses leading to identification of a biochemical role for the moeA (molybdate metabolism) gene product in Escherichia coliThe mononuclear molybdenum enzymes.Comparative calculation of EPR spectral parameters in [Mo(V)OX4]-, [Mo(V)OX5]2-, and [Mo(V)OX4(H2O)]- complexes.A novel sec-independent periplasmic protein translocation pathway in Escherichia coliMolecular analysis of dimethyl sulphide dehydrogenase from Rhodovulum sulfidophilum: its place in the dimethyl sulphoxide reductase family of microbial molybdopterin-containing enzymes.Exploring the evolution of protein function in ArchaeaPyranopterin dithiolene distortions relevant to electron transfer in xanthine oxidase/dehydrogenase.Which functional groups of the molybdopterin ligand should be considered when modeling the active sites of the molybdenum and tungsten cofactors? A density functional theory study.Characterization of metalloproteins by high-throughput X-ray absorption spectroscopy.Thiol-disulfide exchange is involved in the catalytic mechanism of peptide methionine sulfoxide reductaseInteraction of product analogues with the active site of rhodobacter sphaeroides dimethyl sulfoxide reductaseSynthesis, characterization, and spectroscopy of model molybdopterin complexes.Regression modeling of the North East Atlantic Spring Bloom suggests previously unrecognized biological roles for V and Mo.A Model for the Active-Site Formation Process in DMSO Reductase Family Molybdenum Enzymes Involving Oxido-Alcoholato and Oxido-Thiolato Molybdenum(VI) Core Structures.Oxo-carboxylato-molybdenum(VI) complexes possessing dithiolene ligands related to the active site of type II DMSOR family molybdoenzymes.Metalloproteins containing cytochrome, iron-sulfur, or copper redox centersShifting the metallocentric molybdoenzyme paradigm: the importance of pyranopterin coordination.Structural and mechanistic insights on nitrate reductases.The syntheses and characterizations of molybdenum(VI) complexes with catechol and 2,3-dihydroxynaphthalene, and the structure-effect relationship in their in vitro anticancer activities.Isolation of a periplasmic molecular chaperone-like protein of Rhodobacter sphaeroides f. sp. denitrificans that is homologous to the dipeptide transport protein DppA of Escherichia coli.Redox-dependent gene regulation in Rhodobacter sphaeroides 2.4.1(T): effects on dimethyl sulfoxide reductase (dor) gene expression.Mediated electrochemistry of dimethyl sulfoxide reductase from Rhodobacter capsulatus.Characterization of a pre-export enzyme-chaperone complex on the twin-arginine transport pathway.Thiocyanate binding to the molybdenum centre of the periplasmic nitrate reductase from Paracoccus pantotrophus.
P2860
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P2860
Crystal structure of DMSO reductase: redox-linked changes in molybdopterin coordination.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
1996年论文
@zh
1996年论文
@zh-cn
name
Crystal structure of DMSO reductase: redox-linked changes in molybdopterin coordination.
@en
Crystal structure of DMSO reductase: redox-linked changes in molybdopterin coordination.
@nl
type
label
Crystal structure of DMSO reductase: redox-linked changes in molybdopterin coordination.
@en
Crystal structure of DMSO reductase: redox-linked changes in molybdopterin coordination.
@nl
prefLabel
Crystal structure of DMSO reductase: redox-linked changes in molybdopterin coordination.
@en
Crystal structure of DMSO reductase: redox-linked changes in molybdopterin coordination.
@nl
P2093
P1433
P1476
Crystal structure of DMSO reductase: redox-linked changes in molybdopterin coordination.
@en
P2093
Rajagopalan KV
Schindelin H
P304
P356
10.1126/SCIENCE.272.5268.1615
P407
P577
1996-06-01T00:00:00Z