Electronic structure analysis of the oxygen-activation mechanism by Fe(II)- and α-ketoglutarate (αKG)-dependent dioxygenases.
about
Insights into enzymatic halogenation from computational studiesImposing function down a (cupin)-barrel: secondary structure and metal stereochemistry in the αKG-dependent oxygenases.Evidence that the fosfomycin-producing epoxidase, HppE, is a non-heme-iron peroxidaseMechanisms of tryptophan and tyrosine hydroxylase.2-Oxoglutarate-dependent dioxygenases are sensors of energy metabolism, oxygen availability, and iron homeostasis: potential role in the regulation of aging process.The rate-limiting step of O2 activation in the α-ketoglutarate oxygenase factor inhibiting hypoxia inducible factor.Experimental Correlation of Substrate Position with Reaction Outcome in the Aliphatic Halogenase, SyrB2.Substrate Promotes Productive Gas Binding in the α-Ketoglutarate-Dependent Oxygenase FIH.Hydrogen-bonding effects on the reactivity of [X-Fe(III)-O-Fe(IV)═O] (X = OH, F) complexes toward C-H bond cleavage.Spectroscopic Evidence for the Two C-H-Cleaving Intermediates of Aspergillus nidulans Isopenicillin N Synthase.1-Aminocyclopropane-1-carboxylic acid oxidase reaction mechanism and putative post-translational activities of the ACCO proteinMono- and binuclear non-heme iron chemistry from a theoretical perspective.Substrate positioning by Gln(239) stimulates turnover in factor inhibiting HIF, an αKG-dependent hydroxylase.Synthesis, X-ray Structures, Electronic Properties, and O2/NO Reactivities of Thiol Dioxygenase Active-Site Models.Formation and structure of the ferryl [Fe[double bond, length as m-dash]O] intermediate in the non-haem iron halogenase SyrB2: classical and QM/MM modelling agree.Mechanistic insights into dioxygen activation, oxygen atom exchange and substrate epoxidation by AsqJ dioxygenase from quantum mechanical/molecular mechanical calculations.Visualizing the Reaction Cycle in an Iron(II)- and 2-(Oxo)-glutarate-Dependent Hydroxylase.Acid-facilitated product release from a Mo(IV) center: relevance to oxygen atom transfer reactivity of molybdenum oxotransferases.Dioxygen Binding in the Active Site of Histone Demethylase JMJD2A and the Role of the Protein Environment.
P2860
Q26828508-24D875DF-10A1-4EB4-AECB-51408F5C6820Q30155130-5B38A582-8183-400C-A334-99E41B40AF3DQ34163009-EFD88F1B-F6B0-4B92-8C7C-14F9F1F1AFA7Q34329841-43A6ECCC-6BF8-4473-8405-7BF192F18930Q34482634-EDDAC173-BCAB-43A1-9EC8-9C9DBDC96296Q34822239-042EC898-898A-4461-9FC8-8074F044FABEQ35685107-66F41CAD-8CEC-40E0-9102-B55379645ACFQ36691958-79B7E6CA-43E6-433C-9613-998BD867E47CQ36784234-5128F6F9-58DE-4C9E-AC13-4112700BAB55Q37116091-0C8C824C-4B13-43F6-8362-5F41F7AA63F7Q37310031-00259CFE-06FA-4440-8759-95AFB71315F9Q38845297-9FA676E3-21D3-46BC-B71C-2892AE76DA7AQ41903057-52DD906D-1BFB-49C5-9622-305B7837D8D2Q43822806-A9CEBF6B-0270-44E1-9DAB-9EA9790E7CA8Q46269562-28ED276A-0A6B-4CD7-97DB-D22D01D7B452Q46333343-56834110-6185-4EBC-BEF4-77409D827E3FQ47930869-5424912B-8643-4049-AD13-5F30FEBC0B8EQ49607941-4BACE594-20DF-40DD-847B-E0A71DB8942CQ51641598-B1B90BB2-50B3-4486-8459-DC4EC7CF4660
P2860
Electronic structure analysis of the oxygen-activation mechanism by Fe(II)- and α-ketoglutarate (αKG)-dependent dioxygenases.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年学术文章
@wuu
2012年学术文章
@zh-cn
2012年学术文章
@zh-hans
2012年学术文章
@zh-my
2012年学术文章
@zh-sg
2012年學術文章
@yue
2012年學術文章
@zh
2012年學術文章
@zh-hant
name
Electronic structure analysis ...... (αKG)-dependent dioxygenases.
@en
type
label
Electronic structure analysis ...... (αKG)-dependent dioxygenases.
@en
prefLabel
Electronic structure analysis ...... (αKG)-dependent dioxygenases.
@en
P2093
P2860
P356
P1476
Electronic structure analysis ...... (αKG)-dependent dioxygenases.
@en
P2093
Andreas Hansen
Christoph Riplinger
J Martin Bollinger
Shengfa Ye
P2860
P304
P356
10.1002/CHEM.201102829
P407
P577
2012-04-18T00:00:00Z