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Crystal structure of the dioxygen-bound heme oxygenase from Corynebacterium diphtheriae: implications for heme oxygenase functionThe Apolar Channel in Cerebratulus lacteus Hemoglobin Is the Route for O2 Entry and ExitLigand Migration in the Apolar Tunnel of Cerebratulus lacteus Mini-HemoglobinHigh Resolution Crystal Structures of the Cerebratulus lacteus Mini-Hb in the Unligated and Carbomonoxy StatesStructures of K42N and K42Y sperm whale myoglobins point to an inhibitory role of distal water in peroxidase activitySignificantly enhanced heme retention ability of myoglobin engineered to mimic the third covalent linkage by nonaxial histidine to heme (vinyl) in synechocystis hemoglobinCompetition with xenon elicits ligand migration and escape pathways in myoglobin.Diatomic ligand discrimination by the heme oxygenases from Neisseria meningitidis and Pseudomonas aeruginosa.Recombinant hemoglobin II from Lucina pectinata: a large-scale method for hemeprotein expression in E. coliHow do heme-protein sensors exclude oxygen? Lessons learned from cytochrome c', Nostoc puntiforme heme nitric oxide/oxygen-binding domain, and soluble guanylyl cyclase.Thr-E11 regulates O2 affinity in Cerebratulus lacteus mini-hemoglobin.Oxygenated complex of cytochrome bd from Escherichia coli: stability and photolability.Ligand migration through hemeprotein cavities: insights from laser flash photolysis and molecular dynamics simulations.Ligand recombination and a hierarchy of solvent slaved dynamics: the origin of kinetic phases in hemeproteins.Examining and mitigating acellular hemoglobin vasoactivity.Effects of local protein environment on the binding of diatomic molecules to heme in myoglobins. DFT and dispersion-corrected DFT studies.Factors controlling the reactivity of hydrogen sulfide with hemeproteins.Hyperoxia attenuates the inhibitory effect of nitric oxide donors on HIF prolyl-4-hydroxylase-2: Implication on discriminative effect of nitric oxide on HIF prolyl-4-hydroxylase-2 and collagen prolyl-4-hydroxylase.Modulating distal cavities in the α and β subunits of human HbA reveals the primary ligand migration pathway.A "sliding scale rule" for selectivity among NO, CO, and O₂ by heme protein sensors.Disentangling ligand migration and heme pocket relaxation in cytochrome P450cam.On the oxygen reactivity of flavoprotein oxidases: an oxygen access tunnel and gate in brevibacterium sterolicum cholesterol oxidase.Ligand binding to truncated hemoglobin N from Mycobacterium tuberculosis is strongly modulated by the interplay between the distal heme pocket residues and internal water.Analysis of the contribution of the globin and reductase domains to the ligand-binding properties of bacterial haemoglobins.CO rebinding to protoheme: investigations of the proximal and distal contributions to the geminate rebinding barrierThermoglobin, oxygen-avid hemoglobin in a bacterial hyperthermophile.Structural dynamics of myoglobin: ligand migration among protein cavities studied by Fourier transform infrared/temperature derivative spectroscopy.Kinetic modulation in carbonmonoxy derivatives of truncated hemoglobins: the role of distal heme pocket residues and extended apolar tunnel.Structural dynamics of myoglobin: ligand migration and binding in valine 68 mutants.A conserved Val to Ile switch near the heme pocket of animal and bacterial nitric-oxide synthases helps determine their distinct catalytic profiles.Viscosity-dependent relaxation significantly modulates the kinetics of CO recombination in the truncated hemoglobin TrHbN from Mycobacterium tuberculosis.2017 Military Supplement: Current Challenges in the Development of Acellular Hemoglobin Oxygen Carriers by Protein Engineering.The position 68(E11) side chain in myoglobin regulates ligand capture, bond formation with heme iron, and internal movement into the xenon cavities.Distal heme pocket conformers of carbonmonoxy derivatives of Ascaris hemoglobin: evidence of conformational trapping in porous sol-gel matrices.
P2860
Q27643141-95F2D3BF-BEA3-44CD-ABBE-71261A86953CQ27652441-B68D9A81-63A0-4AC7-AB31-1FCBE7318FF3Q27666315-045F07AF-8786-485D-A757-78DC47C81E65Q27671852-743B9DDC-1424-4BF0-99B1-E529CD076989Q27696140-AD5A8515-C3CC-451A-9704-16E4B103A4A3Q28651669-01886E3C-5CE5-4186-80D1-E1B4CD4F6919Q31034382-C3EC07AA-7C7F-4936-AC90-2A6D951ADAF4Q33263176-EE5643EE-E7B3-4AE2-959C-87F303CD3C50Q33866253-721182E9-5C0D-4E4B-B371-001400243552Q34166721-C08C7B93-748F-4E70-BD58-5074526A8022Q34322860-E842CBE0-F379-4BB4-A748-C563357ED4A1Q34441256-461A3741-92D1-4793-A4B7-12A4390C181EQ34754684-51FBCA4B-4FB9-4F4A-8B6C-8C31BD3B23F1Q35988592-3AE1C72F-5580-4FF7-B11A-DF07E2DF96AFQ36801603-9580860E-C838-4D15-9C82-AE0C7B1D6261Q37053226-677EB6CD-FB5C-48C1-AA3E-EB30EAB7B64FQ37273727-D1DB2FEF-97EE-4D10-9052-429DB4392D2EQ37715426-C49630D8-84DB-40E6-8C6D-25E8EC39CDB8Q38256073-015D99D1-0306-4E7B-B72C-6372522B2E91Q40281016-FBF1E615-C5BD-4341-8C97-377D986CE618Q40316220-F4390F95-90C4-4584-94F2-E2EB5878EB4AQ40454299-3CBB20A3-46DF-4483-9FE0-FF416FCC318EQ41985089-466ED12A-40DF-4247-BC69-35314F06DA45Q42066939-E67FB58E-0E72-4504-9D85-102D03199CC7Q42555763-9A7792C0-3C72-49CB-A07D-5F854D60C253Q42666381-D8B11687-BA4B-4AF0-9B58-9AE5EA6AA53CQ43855735-362A08A1-F43F-47C2-A0C2-72B8DB8F07A9Q44433301-57398F2F-16F6-413B-9499-05833B395D55Q44542402-14B09400-32EC-41FF-BC80-9524398794D9Q44771684-FF16ABA2-FE02-418C-8AFA-E932834F4C8DQ44964552-1E7F62F6-EB12-409B-89E1-F2A732F176C0Q46266772-96B9EDBC-0B1E-4BAE-988C-52CBB04E3C16Q46696953-A0A087D8-ED97-4AE0-9E69-152510DFC3A8Q47305676-54BA3A30-2B48-4818-A749-190A8C805398
P2860
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年学术文章
@wuu
2001年学术文章
@zh
2001年学术文章
@zh-cn
2001年学术文章
@zh-hans
2001年学术文章
@zh-my
2001年学术文章
@zh-sg
2001年學術文章
@yue
2001年學術文章
@zh-hant
name
Controlling ligand binding in myoglobin by mutagenesis.
@en
Controlling ligand binding in myoglobin by mutagenesis.
@nl
type
label
Controlling ligand binding in myoglobin by mutagenesis.
@en
Controlling ligand binding in myoglobin by mutagenesis.
@nl
prefLabel
Controlling ligand binding in myoglobin by mutagenesis.
@en
Controlling ligand binding in myoglobin by mutagenesis.
@nl
P2093
P2860
P50
P356
P1476
Controlling ligand binding in myoglobin by mutagenesis.
@en
P2093
Carlo Travaglini-Allocatelli
Federica Draghi
Quentin H Gibson
P2860
P304
P356
10.1074/JBC.M109206200
P407
P577
2001-12-14T00:00:00Z