Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Viscosity-dependent relaxation significantly modulates the kinetics of CO recombination in the truncated hemoglobin TrHbN from Mycobacterium tuberculosis.

The Journal of biological chemistry - 10 Sept 2004

Dantsker David, Samuni Uri, Ouellet Yannick, Wittenberg Beatrice A, Wittenberg Jonathan B, Milani Mario, Bolognesi Martino, Guertin Michel, Friedman Joel M

Abstract excerpt

Kinetic traces were generated for the nanosecond and slower rebinding of photodissociated CO to trHbN in solution and in porous sol-gel matrices as a function of viscosity, conformation, and mutation. TrHbN is one of the two truncated hemoglobins from Mycobacterium tuberculosis. The kinetic traces were analyzed in terms of three distinct phases. These three phases are ascribed to rebinding: (i) from the distal...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Carbon Monoxide
Share to Glycerol

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hemoglobins

Share to Ligands

Share to Models, Chemical

Share to Mycobacterium tuberculosis

Source

Identifiers

PMID: 15234986
DOI: 10.1074/jbc.M401513200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Viscosity-dependent relaxation significantly modulates the kinetics of CO recombination in the truncated hemoglobin TrHbN from Mycobacterium tuberculosis.PMID 15234986Read ↗

Conformational dependence of hemoglobin reactivity under high viscosity conditions: the role of solvent slaved dynamics.Semantic proximity Read ↗

Ligand migration in the truncated hemoglobin-II from Mycobacterium tuberculosis: the role of G8 tryptophan.Semantic proximity Read ↗

The position 68(E11) side chain in myoglobin regulates ligand capture, bond formation with heme iron, and internal movement into the xenon cavities.Semantic proximity Read ↗

A hierarchy of functionally important relaxations within myoglobin based on solvent effects, mutations and kinetic model.Semantic proximity Read ↗

Ligand uptake in Mycobacterium tuberculosis truncated hemoglobins is controlled by both internal tunnels and active site water moleculesSemantic proximity Read ↗

Ligand binding to truncated hemoglobin N from Mycobacterium tuberculosis is strongly modulated by the interplay between the distal heme pocket residues and internal water.Semantic proximity Read ↗

Effect of Occluded Ligand Migration on the Kinetics and Structural Dynamics of Homodimeric Hemoglobin.Semantic proximity Read ↗

Unusually strong H-bonding to the heme ligand and fast geminate recombination dynamics of the carbon monoxide complex of Bacillus subtilis truncated hemoglobin.Semantic proximity Read ↗

Kinetics and computational studies of ligand migration in nitrophorin 7 and its Δ1-3 mutant.Semantic proximity Read ↗

Nitric oxide recombination to double mutants of myoglobin: role of ligand diffusion in a fluctuating heme pocket.Semantic proximity Read ↗

Structural determinants of ligand migration in Mycobacterium tuberculosis truncated hemoglobin OSemantic proximity Read ↗

Ligand-induced protein responses and mechanical signal propagation described by linear response theories.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.