about
Pirin is an iron-dependent redox regulator of NF-κBPurification and characterization of the epoxidase catalyzing the formation of fosfomycin from Pseudomonas syringaeDetermination of the substrate binding mode to the active site iron of (S)-2-hydroxypropylphosphonic acid epoxidase using 17O-enriched substrates and substrate analoguesDefining the Role of the Axial Ligand of the Type 1 Copper Site in Amicyanin by Replacement of Methionine with LeucineProline 96 of the Copper Ligand Loop of Amicyanin Regulates Electron Transfer from Methylamine Dehydrogenase by Positioning Other Residues at the Protein−Protein InterfaceEvidence for a Dual Role of an Active Site Histidine in α-Amino-β-carboxymuconate-ε-semialdehyde DecarboxylaseMutagenesis of tryptophan199 suggests that hopping is required for MauG-dependent tryptophan tryptophylquinone biosynthesisDiradical intermediate within the context of tryptophan tryptophylquinone biosynthesisProline 107 Is a Major Determinant in Maintaining the Structure of the Distal Pocket and Reactivity of the High-Spin Heme of MauGThe Power of Two: ARGININE 51 AND ARGININE 239* FROM A NEIGHBORING SUBUNIT ARE ESSENTIAL FOR CATALYSIS IN -AMINO- -CARBOXYMUCONATE- -SEMIALDEHYDE DECARBOXYLASEYeast ribonucleotide reductase has a heterodimeric iron-radical-containing subunit.Human α-amino-β-carboxymuconate-ε-semialdehyde decarboxylase (ACMSD): a structural and mechanistic unveilingNew paramagnetic species formed at the expense of the transient tyrosyl radical in mutant protein R2 F208Y of Escherichia coli ribonucleotide reductase.EPR and Mössbauer spectroscopy show inequivalent hemes in tryptophan dioxygenase.Development of a CZE-ESI-MS assay with a sulfonated capillary for profiling picolinic acid and quinolinic acid formation in multienzyme systemCrystallographic and spectroscopic snapshots reveal a dehydrogenase in action.Interconversion of two oxidized forms of taurine/alpha-ketoglutarate dioxygenase, a non-heme iron hydroxylase: evidence for bicarbonate binding.Enzyme reactivation by hydrogen peroxide in heme-based tryptophan dioxygenaseProbing bis-Fe(IV) MauG: experimental evidence for the long-range charge-resonance model.What is the tryptophan kynurenine pathway and why is it important to neurotherapeutics?Role of calcium in metalloenzymes: effects of calcium removal on the axial ligation geometry and magnetic properties of the catalytic diheme center in MauG.Improved separation and detection of picolinic acid and quinolinic acid by capillary electrophoresis-mass spectrometry: application to analysis of human cerebrospinal fluid.An Iron Reservoir to the Catalytic Metal: THE RUBREDOXIN IRON IN AN EXTRADIOL DIOXYGENASE.Control of carotenoid biosynthesis through a heme-based cis-trans isomerase.The roles of Rhodobacter sphaeroides copper chaperones PCu(A)C and Sco (PrrC) in the assembly of the copper centers of the aa(3)-type and the cbb(3)-type cytochrome c oxidasesA catalytic di-heme bis-Fe(IV) intermediate, alternative to an Fe(IV)=O porphyrin radical.Tryptophan-mediated charge-resonance stabilization in the bis-Fe(IV) redox state of MauG.Synthesis, characterization, and preliminary in vitro studies of vanadium(IV) complexes with a Schiff base and thiosemicarbazones as mixed-ligandsAn unexpected copper catalyzed 'reduction' of an arylazide to amine through the formation of a nitrene intermediateTryptophan tryptophylquinone biosynthesis: a radical approach to posttranslational modification.Decarboxylation mechanisms in biological system.Heme-dependent dioxygenases in tryptophan oxidation.Bis-Fe(IV): nature's sniper for long-range oxidation.Alpha-amino-beta-carboxymuconic-epsilon-semialdehyde decarboxylase (ACMSD) is a new member of the amidohydrolase superfamily.The anaerobic (class III) ribonucleotide reductase from Lactococcus lactis. Catalytic properties and allosteric regulation of the pure enzyme system.Heterolytic OO bond cleavage: Functional role of Glu113 during bis-Fe(IV) formation in MauG.A Pitcher-and-Catcher Mechanism Drives Endogenous Substrate Isomerization by a Dehydrogenase in Kynurenine Metabolism.A single EF-hand isolated from STIM1 forms dimer in the absence and presence of Ca2+Effects of the loss of the axial tyrosine ligand of the low-spin heme of MauG on its physical properties and reactivity.Mutagenic analysis of Cox11 of Rhodobacter sphaeroides: insights into the assembly of Cu(B) of cytochrome c oxidase.
P50
Q24294125-9F612521-997C-40D5-A46E-5ABE655DDA63Q24653335-2A4BDF6C-0AB1-425E-B265-54D5BDF12A0DQ24653368-26DFF906-E697-478B-B908-F69680A40F26Q27657215-F9C64579-1B9A-4B5E-8B1D-D7FCEBA0DB1FQ27666737-9E31FE9C-F481-4DD7-8CD1-6CD3A83A866BQ27670567-196D8A79-9373-4A02-85E3-DDEA1B679BF9Q27674714-4C995815-88FF-4F6D-89A8-222C8EF9743AQ27676809-55396ABF-2825-49BD-B594-2AE864FAE586Q27677014-35AE2BEB-AB61-46BC-AF9B-23B475D308CFQ27679904-5C8DE99A-B354-4747-81A5-19C407436CF2Q27939596-135157C8-F390-4056-B136-071C177EA609Q28115413-B45A12D7-7E0B-4DD0-ABF0-941C51911C32Q32061682-B94CA609-0407-4908-9079-D7ECF4A606DBQ34090851-9B3675AF-E1BE-40B8-BEB7-951FC712C839Q34128480-6053DBAD-CAEC-480A-964D-BCBD9B58A8FFQ34865894-54F68CEA-CBC1-48AB-BFB7-2695C9DB55C7Q34916802-D1E57754-8F96-464B-A819-F69297B743A5Q35128201-1C12128C-1332-4854-A86D-2D87D78D00A1Q35188543-29F24BD3-E32F-448E-A22B-E428F5938BA9Q35788398-6D24848E-1FFC-4352-AFDA-F17A907468FFQ35804440-2C78771C-436D-4868-BB9A-443C533E2AAAQ35852039-0D34A187-63CE-4D81-B384-25FE97E399CFQ35860669-881BDEC5-F357-42DB-9945-7A3516F58911Q35875500-0EADFBFD-38E4-460F-9729-843ADA7D5920Q35911449-D088CBB2-E6E8-4206-9E87-9981D42A8C5BQ36735315-ECA4F940-099D-4FC3-A337-8FE2442EF126Q36932428-C01ED5D0-FE6F-4AE0-9ABA-4A16339C05C4Q37051991-C042C4B5-2269-4E9E-A6D5-6213EF49572DQ37119795-D260CA88-10C1-4A33-941F-97A1ACDB6465Q37982234-23C5CF60-D571-4AF6-96C1-E7E0DAB59FE6Q38005515-3CD57EE8-FC4F-440A-B81E-DC9A80A4721BQ38167965-3DEBF774-DD17-49DE-B4D5-B496B3E87E19Q38203816-D552791A-6D70-4983-A9D2-03526DE1E5FFQ38313071-4C1C39FA-7307-4A59-9C8A-359F4A397850Q38316304-A96D01CF-0320-4E16-B765-550E8BA0D57DQ39138975-3903EA32-1797-4ED8-B072-74CF50E4954AQ39218665-40A1E6DD-823D-40E1-81F2-BCC11E941310Q40421995-A3574C1C-9070-44B3-96B5-1F86E46DE4F3Q40645644-EFDD4FF3-141B-4430-85D2-09AF54B6B8E2Q41375098-BEF75FDF-28DE-46EE-A55D-6EC2AB8BB299
P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Aimin Liu
@ast
Aimin Liu
@en
Aimin Liu
@es
Aimin Liu
@nl
type
label
Aimin Liu
@ast
Aimin Liu
@en
Aimin Liu
@es
Aimin Liu
@nl
altLabel
Feradical
@en
prefLabel
Aimin Liu
@ast
Aimin Liu
@en
Aimin Liu
@es
Aimin Liu
@nl
P1053
C-1572-2017
P106
P1153
55793189196
P31
P3829
P496
0000-0002-4182-8176