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

Structural and biochemical characterization of two heme binding sites on α1-microglobulin using site directed mutagenesis and molecular simulation.

Biochimica et biophysica acta - 1 Jan 2016

Rutardottir Sigurbjörg, Karnaukhova Elena, Nantasenamat Chanin, Songtawee Napat, Prachayasittikul Virapong, Rajabi Mohsen, Rosenlöf Lena Wester, Alayash Abdu I, Åkerström Bo

Abstract excerpt

BACKGROUND: α1-Microglobulin (A1M) is a reductase and radical scavenger involved in physiological protection against oxidative damage. These functions were previously shown to be dependent upon cysteinyl-, C34, and lysyl side-chains, K(92, 118,130). A1M binds heme and the crystal structure suggests that C34 and H123 participate in a heme binding site. We have investigated the involvement of these five residues in...

Read the complete abstract on PubMed

Topics

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

Share to Alpha-Globulins
Share to Circular Dichroism

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

Share to Molecular Dynamics Simulation

Share to Mutagenesis, Site-Directed

Share to Oxidation-Reduction

Share to Spectrometry, Fluorescence

Share to Surface Plasmon Resonance

Source

Identifiers

PMID: 26497278
DOI: 10.1016/j.bbapap.2015.10.002

Genes

SPR

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural and biochemical characterization of two heme binding sites on α1-microglobulin using site directed mutagenesis and molecular simulation.PMID 26497278Read ↗

Production of recombinant human alpha1-microglobulin and mutant forms involved in chromophore formation.Semantic proximity Read ↗

Redox properties of the lipocalin alpha1-microglobulin: reduction of cytochrome c, hemoglobin, and free iron.Semantic proximity Read ↗

Structure, Functions, and Physiological Roles of the Lipocalin α1-Microglobulin (A1M)Semantic proximity Read ↗

Human haptoglobin structure and function--a molecular modelling study.Semantic proximity Read ↗

Protein stability and mutations in the axial methionine loop of a minimal cytochrome c.Semantic proximity Read ↗

Effect of a K72A Mutation on the Structure, Stability, Dynamics, and Peroxidase Activity of Human Cytochrome c.Semantic proximity Read ↗

Effect of conservative mutations (L94V and L94I) on the structure and stability of horse cytochrome c.Semantic proximity Read ↗

Exploring the molecular basis of human manganese superoxide dismutase inactivation mediated by tyrosine 34 nitration.Semantic proximity Read ↗

Distinct roles of a tyrosine-associated hydrogen-bond network in fine-tuning the structure and function of heme proteins: two cases designed for myoglobin.Semantic proximity Read ↗

Effects of natural mutations (L94I and L94V) on the stability and mechanism of folding of horse cytochrome c: A combined in vitro and molecular dynamics simulations approach.Semantic proximity Read ↗

A cis-proline in alpha-hemoglobin stabilizing protein directs the structural reorganization of alpha-hemoglobin.Semantic proximity Read ↗

The evolutionary footprint of histidine in hemoglobin and myoglobin: an implication towards their function.Semantic proximity Read ↗

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