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

Effects of mutations in active site heme ligands on the spectroscopic and catalytic properties of SoxAX cytochromes.

Journal of inorganic biochemistry - 1 Sept 2016

Kilmartin James R, Bernhardt Paul V, Dhouib Rabeb, Hanson Graeme R, Riley Mark J, Kappler Ulrike

Abstract excerpt

By attaching a sulfur substrate to a conserved cysteine of the SoxYZ carrier protein SoxAX cytochromes initiate the reaction cycle of the Sox (sulfur oxidation) multienzyme complex, which is the major pathway for microbial reoxidation of sulfur compounds in the environment. Despite their important role in this process, the reaction mechanism of the SoxAX cytochromes has not been fully elucidated. Here we report...

Read the complete abstract on PubMed

Topics

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

Share to Biocatalysis
Share to Catalytic Domain

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

Share to Copper

Share to Cysteine

Share to Cytochromes

Share to Rhizobiaceae

Share to Rhodobacter capsulatus

Source

Identifiers

PMID: 27112898
DOI: 10.1016/j.jinorgbio.2016.04.015

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

Effects of mutations in active site heme ligands on the spectroscopic and catalytic properties of SoxAX cytochromes.PMID 27112898Read ↗

Cytochrome c551 from Starkeya novella: characterization, spectroscopic properties, and phylogeny of a diheme protein of the SoxAX family.Semantic proximity Read ↗

Redox signal transduction: mutations shifting [2Fe-2S] centers of the SoxR sensor-regulator to the oxidized form.Semantic proximity Read ↗

Kinetic and structural evidence for the importance of Tyr236 for the integrity of the Mo active site in a bacterial sulfite dehydrogenase.Semantic proximity Read ↗

Anatomy of a red copper center: spectroscopic identification and reactivity of the copper centers of Bacillus subtilis Sco and its Cys-to-Ala variants.Semantic proximity Read ↗

Functional analysis of SoxR residues affecting transduction of oxidative stress signals into gene expression.Semantic proximity Read ↗

A structural study towards the understanding of the interactions of SoxY, SoxZ, and SoxB, leading to the oxidation of sulfur anions via the novel global sulfur oxidizing (sox) operon.Semantic proximity Read ↗

Trp180 of endothelial NOS and Trp56 of bacterial saNOS modulate sigma bonding of the axial cysteine to the heme.Semantic proximity Read ↗

A reducing system of the superoxide sensor SoxR in Escherichia coli.Semantic proximity Read ↗

The cytochrome complex SoxXA of Paracoccus pantotrophus is produced in Escherichia coli and functional in the reconstituted sulfur-oxidizing enzyme system.Semantic proximity Read ↗

Structural Adaptability Facilitates Histidine Heme Ligation in a Cytochrome P450.Semantic proximity Read ↗

Exploring second coordination sphere effects in nitric oxide synthase.Semantic proximity Read ↗

A comprehensive alanine scanning mutagenesis of the Escherichia coli transcriptional activator SoxS: identifying amino acids important for DNA binding and transcription activation.Semantic proximity Read ↗

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