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

Unusual pressure effects on ligand rebinding to the human myoglobin Leucine 29 mutants.

The Journal of biological chemistry - 29 Sept 2000

Uchida T, Ishimori K, Morishima I

Abstract excerpt

Using high pressure flash photolysis, we revealed that the side chain of Leu(29) controls the reaction volume of the ligand migration process in myoglobin, which is the primary factor for the unusual activation volume of ligand binding in some Leu(29) mutants. As we previously reported (Adachi, S., Sunohara, N., Ishimori, K., and Morishima, I. (1992) J. Biol. Chem. 267, 12614-12621), CO bimolecular rebinding in...

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 Hydrostatic Pressure
Share to Leucine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Ligands

Share to Models, Chemical

Share to Myoglobin

Share to Oxygen

Share to Photolysis

Source

Identifiers

PMID: 10906339
DOI: 10.1074/jbc.M910287199

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

Unusual pressure effects on ligand rebinding to the human myoglobin Leucine 29 mutants.PMID 10906339Read ↗

The effects of the L29F mutation on the ligand migration kinetics in crystallized myoglobin as revealed by molecular dynamics simulations.Semantic proximity Read ↗

Ligand migration and protein fluctuations in myoglobin mutant L29W.Semantic proximity Read ↗

Myoglobin mutants giving the largest geminate yield in CO rebinding in the nanosecond time domain.Semantic proximity Read ↗

Primary protein response after ligand photodissociation in carbonmonoxy myoglobin.Semantic proximity Read ↗

Structural dynamics of ligand diffusion in the protein matrix: A study on a new myoglobin mutant Y(B10) Q(E7) R(E10).Semantic proximity Read ↗

Anatomy and dynamics of a ligand-binding pathway in myoglobin: the roles of residues 45, 60, 64, and 68.Semantic proximity Read ↗

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

An engineered heme-copper center in myoglobin: CO migration and binding.Semantic proximity Read ↗

Ligand pathways in myoglobin: a review of Trp cavity mutations.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 ↗

Molecular mechanism of myoglobin autoxidation: insights from computer simulations.Semantic proximity Read ↗

Structural and functional effects of apolar mutations of the distal valine in myoglobin.Semantic proximity Read ↗

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