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

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

Biochemistry - 6 Sept 1994

Carlson M L, Regan R, Elber R, Li H, Phillips G N, Olson J S, Gibson Q H

Abstract excerpt

Picosecond recombination of nitric oxide to the double mutants of myoglobin, His64Gly-Val68Ala and His64Gly.Val68Ile, at E7 and E11, has been studied experimentally and by computation. It is shown that distal residues have a profound effect on NO recombination. Recombination in the mutants may be explained in terms of fluctuating free volume and structure of the heme pocket. The double mutants provide insight...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Heme
Share to Ligands

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Models, Molecular

Share to Molecular Sequence Data

Share to Mutation

Share to Recombinant Proteins

Share to Structure-Activity Relationship

Source

Identifiers

PMID: 8075059
DOI: 10.1021/bi00201a005

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Nitric oxide recombination to double mutants of myoglobin: role of ligand diffusion in a fluctuating heme pocket.PMID 8075059Read ↗

Ultrafast measurements of geminate recombination of NO with site-specific mutants of human 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 ↗

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 ↗

Multiphoton absorption of myoglobin-nitric oxide complex: relaxation by D-NEMD of a stationary state.Semantic proximity Read ↗

Distal cavity fluctuations in myoglobin: protein motion and ligand diffusion.Semantic proximity Read ↗

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

Distal Val346Ile mutation in inducible NO synthase promotes substrate-dependent NO confinement.Semantic proximity Read ↗

Ligand diffusion in the distal heme pocket of myoglobin. A primary determinant of geminate rebinding.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 ↗

Structural dynamics of myoglobin.Semantic proximity Read ↗

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

Human myoglobin recognition of oxygen: dynamics of the energy landscape.Semantic proximity Read ↗

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