Viscosity-dependent relaxation significantly modulates the kinetics of CO recombination in the truncated hemoglobin TrHbN from Mycobacterium tuberculosis.
about
The pH dependence of heme pocket hydration and ligand rebinding kinetics in photodissociated carbonmonoxymyoglobin.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.Proximal influences in two-on-two globins: effect of the Ala69Ser replacement on Synechocystis sp. PCC 6803 hemoglobinRole of PheE15 gate in ligand entry and nitric oxide detoxification function of mycobacterium tuberculosis truncated hemoglobin N.Ligand binding to truncated hemoglobin N from Mycobacterium tuberculosis is strongly modulated by the interplay between the distal heme pocket residues and internal water.
P2860
Viscosity-dependent relaxation significantly modulates the kinetics of CO recombination in the truncated hemoglobin TrHbN from Mycobacterium tuberculosis.
description
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name
Viscosity-dependent relaxation ...... om Mycobacterium tuberculosis.
@en
Viscosity-dependent relaxation ...... om Mycobacterium tuberculosis.
@nl
type
label
Viscosity-dependent relaxation ...... om Mycobacterium tuberculosis.
@en
Viscosity-dependent relaxation ...... om Mycobacterium tuberculosis.
@nl
prefLabel
Viscosity-dependent relaxation ...... om Mycobacterium tuberculosis.
@en
Viscosity-dependent relaxation ...... om Mycobacterium tuberculosis.
@nl
P2093
P2860
P356
P1476
Viscosity-dependent relaxation ...... om Mycobacterium tuberculosis.
@en
P2093
Beatrice A Wittenberg
David Dantsker
Joel M Friedman
Jonathan B Wittenberg
Michel Guertin
Uri Samuni
Yannick Ouellet
P2860
P304
38844-38853
P356
10.1074/JBC.M401513200
P407
P577
2004-07-01T00:00:00Z