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

Catalytic activity, stability, unfolding, and degradation pathways of engineered and reconstituted myoglobins.

Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry - 1 Jan 2005

Roncone Raffaella, Monzani Enrico, Labò Sara, Sanangelantoni Anna Maria, Casella Luigi

Abstract excerpt

The structural and functional consequences of engineering a positively charged Lys residue and replacing the natural heme with a heme-L-His derivative in the active site of sperm whale myoglobin (Mb) have been investigated. The main structural change caused by the distal T67K mutation appears to be mobilization of the propionate-7 group. Reconstitution of wild-type and T67K Mb with heme-L-His relaxes the protein...

Read the complete abstract on PubMed

Topics

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

Share to Catalysis
Share to Chromatography, High Pressure Liquid

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

Share to Guanidine

Share to Magnetic Resonance Spectroscopy

Share to Myoglobin

Share to Protein Denaturation

Share to Protein Engineering

Share to Whales

Source

Identifiers

PMID: 15565498
DOI: 10.1007/s00775-004-0606-4

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

Catalytic activity, stability, unfolding, and degradation pathways of engineered and reconstituted myoglobins.PMID 15565498Read ↗

Hybridization of modified-heme reconstitution and distal histidine mutation to functionalize sperm whale myoglobin.Semantic proximity Read ↗

Stability of myoglobin: a model for the folding of heme proteins.Semantic proximity Read ↗

Intra- and intermolecular transfers of protein radicals in the reactions of sperm whale myoglobin with hydrogen peroxide.Semantic proximity Read ↗

Pseudoperoxidase activity, conformational stability, and aggregation propensity of the His98Tyr myoglobin variant: implications for the onset of myoglobinopathy.Semantic proximity Read ↗

Redox reactivity of the heme Fe3+/Fe 2+ couple in native myoglobins and mutants with peroxidase-like activity.Semantic proximity Read ↗

Amyloid fibril formation by circularly permuted and C-terminally deleted mutants.Semantic proximity Read ↗

The mechanism of autooxidation of myoglobin.Semantic proximity Read ↗

The role of copper and protons in heme-copper oxidases: kinetic study of an engineered heme-copper center in myoglobin.Semantic proximity Read ↗

Fast purification of the Apo form and of a non-binding heme mutant of recombinant sperm whale myoglobin.Semantic proximity Read ↗

Regulation of both the structure and function by a de novo designed disulfide bond: a case study of heme proteins in myoglobin.Semantic proximity Read ↗

Significantly enhanced heme retention ability of myoglobin engineered to mimic the third covalent linkage by nonaxial histidine to heme (vinyl) in synechocystis hemoglobin.Semantic proximity Read ↗

Redox instability and hemin loss of mutant sperm whale myoglobins induced by 4-hydroxynonenal in vitro.Semantic proximity Read ↗

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