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

Understanding how the distal environment directs reactivity in chlorite dismutase: spectroscopy and reactivity of Arg183 mutants.

Biochemistry - 6 Mar 2012

Blanc Béatrice, Mayfield Jeffery A, McDonald Claudia A, Lukat-Rodgers Gudrun S, Rodgers Kenton R, DuBois Jennifer L

Abstract excerpt

The chlorite dismutase from Dechloromonas aromatica (DaCld) catalyzes the highly efficient decomposition of chlorite to O(2) and chloride. Spectroscopic, equilibrium thermodynamic, and kinetic measurements have indicated that Cld has two pH sensitive moieties; one is the heme, and Arg183 in the distal heme pocket has been hypothesized to be the second. This active site residue has been examined by site-directed...

Read the complete abstract on PubMed

Topics

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

Share to Arginine
Share to Catalysis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Catalytic Domain

Share to Hydrogen Bonding

Share to Kinetics

Share to Oxidoreductases

Share to Spectrum Analysis, Raman

Share to Structure-Activity Relationship

Source

Open in PubMed Open full text

Identifiers

PMID: 22313119
DOI: 10.1021/bi2017377
PMCID: PMC3369218

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Understanding how the distal environment directs reactivity in chlorite dismutase: spectroscopy and reactivity of Arg183 mutants.PMID 22313119Read ↗

Understanding the roles of strictly conserved tryptophan residues in O2 producing chlorite dismutases.Semantic proximity Read ↗

Structural and denaturation studies of two mutants of a cold adapted superoxide dismutase point to the importance of electrostatic interactions in protein stability.Semantic proximity Read ↗

Investigation of ion binding in chlorite dismutases by means of molecular dynamics simulations.Semantic proximity Read ↗

Apolar distal pocket mutants of yeast cytochrome c peroxidase: hydrogen peroxide reactivity and cyanide binding of the TriAla, TriVal, and TriLeu variants.Semantic proximity Read ↗

Effects of substrate, protein environment, and proximal ligand mutation on compound I and compound 0 of chloroperoxidase.Semantic proximity Read ↗

The role of the distal histidine in H2O2 activation and heme protection in both peroxidase and globin functions.Semantic proximity Read ↗

The Catalase Activity of Catalase-Peroxidases Is Modulated by Changes in the pKa of the Distal Histidine.Semantic proximity Read ↗

Crystal structure of aldoxime dehydratase and its catalytic mechanism involved in carbon-nitrogen triple-bond synthesis.Semantic proximity Read ↗

Distal-to-proximal NO conversion in hemoproteins: the role of the proximal pocket.Semantic proximity Read ↗

pH-dependent properties of a mutant horseradish peroxidase isoenzyme C in which Arg38 has been replaced with lysine.Semantic proximity Read ↗

Chloride regulation of enzyme turnover: application to the role of chloride in photosystem II.Semantic proximity Read ↗

Impact of distal side water and residue 315 on ligand binding to ferric Mycobacterium tuberculosis catalase-peroxidase (KatG).Semantic proximity Read ↗

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