About: Herbicide-Degrading α-Keto Acid-Dependent Enzyme TfdA: Metal Coordination Environment and Mechanistic Insights†

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About: Herbicide-Degrading α-Keto Acid-Dependent Enzyme TfdA: Metal Coordination Environment and Mechanistic Insights† Goto Sponge NotDistinct Permalink

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rdf:type	Item
description	article (en) հոդված (hy) artículu científicu (ast) wetenschappelijk artikel (nl) наукова стаття, опублікована в грудні 1999 (uk) article scientifique publié en 1999 (fr) im Dezember 1999 veröffentlicher wissenschaftlicher Artikel (de)
publication date	wds:Q57831110-595F23BD-7D19-4815-AE79-0DAA9C22E459
publication date	1999-12-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q57831110-813561DE-DB0C-4FC2-8BD9-1C065661B8A7
language of work or name	English
author name string	wds:Q57831110-076FB07E-30AC-4A08-872C-B323B4293078 wds:Q57831110-0B57E2EF-EF6B-4BC6-A374-AC755A236FB7 wds:Q57831110-429C5900-2792-4F44-88D9-73FBEE412323 wds:Q57831110-7AE18F26-4035-414B-B2A0-7AE121D836E2 wds:Q57831110-9AB96B9E-10CF-4E94-95A3-39CE3827C15D
author name string	L Que A K Whiting E L Hegg J McCracken R E Saari
rdfs:label	Herbicide-Degrading α-Keto Acid-Dependent Enzyme TfdA: Metal Coordination Environment and Mechanistic Insights† (en) Herbicide-Degrading α-Keto Acid-Dependent Enzyme TfdA: Metal Coordination Environment and Mechanistic Insights† (nl)
skos:prefLabel	Herbicide-Degrading α-Keto Acid-Dependent Enzyme TfdA: Metal Coordination Environment and Mechanistic Insights† (en) Herbicide-Degrading α-Keto Acid-Dependent Enzyme TfdA: Metal Coordination Environment and Mechanistic Insights† (nl)
name	Herbicide-Degrading α-Keto Acid-Dependent Enzyme TfdA: Metal Coordination Environment and Mechanistic Insights† (en) Herbicide-Degrading α-Keto Acid-Dependent Enzyme TfdA: Metal Coordination Environment and Mechanistic Insights† (nl)
author	wds:Q57831110-A0F33826-E382-4255-BF53-5207738DDBF7
author	Robert Hausinger
title	wds:Q57831110-E7D54CAD-04B2-4333-BCFC-3EC261A98579
title	Herbicide-degrading alpha-keto acid-dependent enzyme TfdA: metal coordination environment and mechanistic insights (en)
page(s)	wds:Q57831110-47D270D0-DCB8-4216-B7B0-523BB31C8D9C
page(s)	16714-16726
instance of	wds:Q57831110-96E06732-0B64-41A1-90E5-D78F2F5DFDCC
instance of	scholarly article
main subject	wds:Q57831110-7FE4ECC5-61DD-40B9-88BF-01535AB31738
main subject	herbicide
PubMed ID	wds:Q57831110-BE1949B3-DB8C-4513-B42D-F4680C58A45F
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/10600135
PubMed ID	10600135
published in	wds:Q57831110-004E7B81-4E2C-497A-8BE3-FC9BC39F1237
published in	Biochemistry
issue	wds:Q57831110-07F57ED7-61A7-4D84-8E7F-A901BF970D64
volume	wds:Q57831110-B760886A-F5FC-4687-96B6-BA9B1F222F66
issue	50
volume	38
DOI	wds:Q57831110-F3119A32-5F32-4F32-A00C-234F763024B1
DOI	http://dx.doi.org/10.1021/BI991796L
DOI	10.1021/BI991796L
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q57831110
is cites work of	Non-heme iron oxygenases Fe(II)/alpha-ketoglutarate hydroxylases involved in nucleobase, nucleoside, nucleotide, and chromatin metabolism Oxidative demethylation by Escherichia coli AlkB directly reverts DNA base damage Interconversion of two oxidized forms of taurine/alpha-ketoglutarate dioxygenase, a non-heme iron hydroxylase: evidence for bicarbonate binding Crystal structures of catalytic complexes of the oxidative DNA/RNA repair enzyme AlkB Oxygen requirement for the biosynthesis of the S-2-hydroxymyristate moiety in Salmonella typhimurium lipid A. Function of LpxO, A new Fe2+/alpha-ketoglutarate-dependent dioxygenase homologue Coordination changes and auto-hydroxylation of FIH-1: uncoupled O2-activation in a human hypoxia sensor. NO reduction by nitric-oxide reductase from denitrifying bacterium Pseudomonas aeruginosa: characterization of reaction intermediates that appear in the single turnover cycle Purification and characterization of the FeII- and alpha-ketoglutarate-dependent xanthine hydroxylase from Aspergillus nidulans The AlkB Family of Fe(II)/α-Ketoglutarate-dependent Dioxygenases: Repairing Nucleic Acid Alkylation Damage and Beyond Cryoreduction of the NO-adduct of taurine:alpha-ketoglutarate dioxygenase (TauD) yields an elusive {FeNO}(8) species Structural basis for the enantiospecificities of R- and S-specific phenoxypropionate/alpha-ketoglutarate dioxygenases Site-directed Mutagenesis of 2,4-Dichlorophenoxyacetic Acid/α-Ketoglutarate Dioxygenase Spectroscopic studies of the mononuclear non-heme Fe(II) enzyme FIH: second-sphere contributions to reactivity Intrinsic tryptophan fluorescence as a probe of metal and alpha-ketoglutarate binding to TfdA, a mononuclear non-heme iron dioxygenase Characterization of a sulfur-regulated oxygenative alkylsulfatase from Pseudomonas putida S-313. Identification and characterization of a unique cysteine residue proximal to the catalytic site of Arabidopsis thaliana carotenoid cleavage enzyme 1. Iopromide exposure in Typha latifolia L.: Evaluation of uptake, translocation and different transformation mechanisms in planta. Characterization of a Trypanosoma brucei Alkb homolog capable of repairing alkylated DNA Spectroscopic and computational studies of reversible O2 binding by a cobalt complex of relevance to cysteine dioxygenase Substrate Promotes Productive Gas Binding in the α-Ketoglutarate-Dependent Oxygenase FIH. The facial triad in the α-ketoglutarate dependent oxygenase FIH: A role for sterics in linking substrate binding to O2 activation Chloride Supports O2 Activation in the D201G Facial Triad Variant of Factor-Inhibiting Hypoxia Inducible Factor, an α-Ketoglutarate Dependent Oxygenase The second coordination sphere of FIH controls hydroxylation. FET3P, ceruloplasmin, and the role of copper in iron metabolism Isolation and biochemical characterization of hypophosphite/2-oxoglutarate dioxygenase. A novel phosphorus-oxidizing enzyme from Psuedomonas stutzeri WM88. Metal and substrate binding to an Fe(II) dioxygenase resolved by UV spectroscopy with global regression analysis Cr(II) reactivity of taurine/alpha-ketoglutarate dioxygenase From Suicide Enzyme to Catalyst: The Iron-Dependent Sulfide Transfer in Methanococcus jannaschii Thiamin Thiazole Biosynthesis Substrate positioning by Gln(239) stimulates turnover in factor inhibiting HIF, an αKG-dependent hydroxylase Chiral hydroxylation at the mononuclear nonheme Fe(II) center of 4-(S) hydroxymandelate synthase--a structure-activity relationship analysis. Novel α-ketoglutarate dioxygenase tfdA-related genes are found in soil DNA after exposure to phenoxyalkanoic herbicides Microbial degradation of halogenated aromatics: molecular mechanisms and enzymatic reactions Glutarate L-2-hydroxylase (CsiD/GlaH) is an archetype Fe(II)/2-oxoglutarate-dependent dioxygenase
is cites work of	wds:Q36458400-0B992E43-FE47-44E9-9F19-AAFF362C213E wds:Q35978195-4E829DE8-1A40-42EA-9CA0-2A4BCEF60C35 wds:Q44284961-F48C829E-913A-4314-9B4F-2271A354F9A2 wds:Q48005110-2DFEE718-339A-4D56-A44C-F8AAB8DB3A3E wds:Q57831109-FC3725CF-46FF-44D5-B32A-1C41E1BD5CD3 wds:Q91721927-D6D14A92-BB1F-4D66-86AC-B5BF1AC3924B wds:Q41168077-487B450A-084B-4A00-A67A-C65CCD005F13 wds:Q41903057-EFBDE46C-4EA2-4E7F-82B7-1AA5447E77BA wds:Q47842357-0AF3BDAD-3F6D-4FB1-A82E-CA077D1676C1 wds:Q28201532-6D37B39D-1544-46E0-825A-B0F87CB772BF wds:Q36691958-F5E78A51-F032-426A-8FA0-71BBDC8D8767 wds:Q41969942-8AA60F52-568D-48CF-9C7C-25B81F1FD138 wds:Q42719732-B5933FE1-FE83-4D8D-8775-35971D346076 wds:Q90360030-1A3191CC-1AFE-4CB4-81F6-B2E76C259292 wds:Q34916802-20F2D1FC-EC0D-4C5A-A413-4F2E520AC824

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