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

Spectroscopic and computational investigation of second-sphere contributions to redox tuning in Escherichia coli iron superoxide dismutase.

Inorganic chemistry - 19 May 2008

Grove Laurie E, Xie Juan, Yikilmaz Emine, Miller Anne-Frances, Brunold Thomas C

Abstract excerpt

In Fe- and Mn-dependent superoxide dismutases (SODs), second-sphere residues have been implicated in precisely tuning the metal ion reduction potential to maximize catalytic activity (Vance, C. K.; Miller, A.-F. J. Am. Chem. Soc. 1998, 120, 461-467). In the present study, spectroscopic and computational methods were used to characterize three distinct Fe-bound SOD species that possess different...

Read the complete abstract on PubMed

Topics

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

Share to Circular Dichroism
Share to Electrons

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hydrogen Bonding

Share to Image Processing, Computer-Assisted

Share to Oxidation-Reduction

Share to Solvents

Share to Spectrophotometry

Share to Superoxide Dismutase

Source

Open in PubMed Open full text

Identifiers

PMID: 18433120
DOI: 10.1021/ic702412y
PMCID: PMC6468990

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

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

Spectroscopic and computational investigation of second-sphere contributions to redox tuning in Escherichia coli iron superoxide dismutase.PMID 18433120Read ↗

The crucial importance of chemistry in the structure-function link: manipulating hydrogen bonding in iron-containing superoxide dismutase.Semantic proximity Read ↗

An evolutionary path to altered cofactor specificity in a metalloenzyme.Semantic proximity Read ↗

Key Structural Motifs Balance Metal Binding and Oxidative Reactivity in a Heterobimetallic Mn/Fe Protein.Semantic proximity Read ↗

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

Spectroscopic and computational investigation of three Cys-to-Ser mutants of nickel superoxide dismutase: insight into the roles played by the Cys2 and Cys6 active-site residues.Semantic proximity Read ↗

Modulation of the heme electronic structure and cystathionine beta-synthase activity by second coordination sphere ligands: The role of heme ligand switching in redox regulation.Semantic proximity Read ↗

Molecular mechanism of myoglobin autoxidation: insights from computer simulations.Semantic proximity Read ↗

Atomic resolution structures of rieske iron-sulfur protein: role of hydrogen bonds in tuning the redox potential of iron-sulfur clusters.Semantic proximity Read ↗

Modulation of function in a minimalist heme-binding membrane protein.Semantic proximity Read ↗

Superoxide reduction by Nanoarchaeum equitans neelaredoxin, an enzyme lacking the highly conserved glutamate iron ligand.Semantic proximity Read ↗

Hydrogen bonding to the cysteine ligand of superoxide reductase: acid-base control of the reaction intermediates.Semantic proximity Read ↗

Elucidating the role of the proximal cysteine hydrogen-bonding network in ferric cytochrome P450cam and corresponding mutants using magnetic circular dichroism spectroscopy.Semantic proximity Read ↗

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