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

Mutual synergy between catalase and peroxidase activities of the bifunctional enzyme KatG is facilitated by electron hole-hopping within the enzyme.

The Journal of biological chemistry - 10 Nov 2017

Njuma Olive J, Davis Ian, Ndontsa Elizabeth N, Krewall Jessica R, Liu Aimin, Goodwin Douglas C

Abstract excerpt

KatG is a bifunctional, heme-dependent enzyme in the front-line defense of numerous bacterial and fungal pathogens against H2O2-induced oxidative damage from host immune responses. Contrary to the expectation that catalase and peroxidase activities should be mutually antagonistic, peroxidatic electron donors (PxEDs) enhance KatG catalase activity. Here, we establish the mechanism of synergistic cooperation...

Read the complete abstract on PubMed

Topics

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

Share to Benzothiazoles
Share to Biocatalysis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Catalase

Share to Electron Spin Resonance Spectroscopy

Share to Electron Transport

Share to Free Radical Scavengers

Share to Peroxidase

Share to Sulfonic Acids

Source

Open in PubMed Open full text

Identifiers

PMID: 28972181
DOI: 10.1074/jbc.M117.791202
PMCID: PMC5682954

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mutual synergy between catalase and peroxidase activities of the bifunctional enzyme KatG is facilitated by electron hole-hopping within the enzyme.PMID 28972181Read ↗

Characterization of the W321F mutant of Mycobacterium tuberculosis catalase-peroxidase KatG.Semantic proximity Read ↗

Engineering tyrosine-based electron flow pathways in proteins: the case of aplysia myoglobin.Semantic proximity Read ↗

Two alternative substrate paths for compound I formation and reduction in catalase-peroxidase KatG from Burkholderia pseudomallei.Semantic proximity Read ↗

Mutational dissection of a hole hopping route in a lytic polysaccharide monooxygenase (LPMO).Semantic proximity Read ↗

Why do bacteria use so many enzymes to scavenge hydrogen peroxide?Semantic proximity Read ↗

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

The role of distal tryptophan in the bifunctional activity of catalase-peroxidases.Semantic proximity Read ↗

Interaction with the Redox Cofactor MYW and Functional Role of a Mobile Arginine in Eukaryotic Catalase-Peroxidase.Semantic proximity Read ↗

Catalases are NAD(P)H-dependent tellurite reductases.Semantic proximity Read ↗

An anaerobic bacterium, Bacteroides thetaiotaomicron, uses a consortium of enzymes to scavenge hydrogen peroxide.Semantic proximity Read ↗

Evolution of Catalases from Bacteria to HumansSemantic proximity Read ↗

Tsa1 is the dominant peroxide scavenger and a source of H2O2-dependent GSSG production in yeast.Semantic proximity Read ↗

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