ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2005
EPR analysis of multiple forms of [4Fe-4S](3+) clusters in HiPIPs.
Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 31 citations in OpenAlex.
- Article
- TheMolecules (Basel, Switzerland) · 2025Review
- Redox-State-Dependent Structural Changes within a Prokaryotic 6-4 Photolyase.Journal of the American Chemical Society · 2025Article
- Distinct Valence States of the [4Fe4S] Cluster Revealed in the Hydrogenase CrHydA1.Angewandte Chemie (International ed. in English) · 2025Article
- Electronic isomerism in a heterometallic nickel-iron-sulfur cluster models substrate binding and cyanide inhibition of carbon monoxide dehydrogenase.Chemical science · 2024Article
- The Cryptic Nature of Fe-S Clusters: A Case Study of the Hepatitis B HBx Oncoprotein.Inorganics · 2023Article
- Electron inventory of the iron-sulfur scaffold complex HypCD essential in [NiFe]-hydrogenase cofactor assembly.The Biochemical journal · 2021Article
- Characterization of Paramagnetic Iron-Sulfur Clusters Using Electron Paramagnetic Resonance Spectroscopy.Methods in molecular biology (Clifton, N.J.) · 2021Article
- The FeoC [4Fe-4S] Cluster Is Redox-Active and Rapidly Oxygen-Sensitive.Biochemistry · 2019Article
- Advanced paramagnetic resonance spectroscopies of iron-sulfur proteins: Electron nuclear double resonance (ENDOR) and electron spin echo envelope modulation (ESEEM).Biochimica et biophysica acta · 2015Review
- Metalloproteins containing cytochrome, iron-sulfur, or copper redox centers.Chemical reviews · 2014Review
- Nonredundant roles for cytochrome c2 and two high-potential iron-sulfur proteins in the photoferrotroph Rhodopseudomonas palustris TIE-1.Journal of bacteriology · 2014Article
- Pyrococcus furiosus 4Fe-ferredoxin, chemisorbed on gold, exhibits gated reduction and ionic strength dependent dimerization.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2006Article
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8 authors at 7 institutions in 4 countries.
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Abstract
The electron paramagnetic resonance (EPR) spectrum from the [4Fe-4S](3+) cluster in several high-potential iron-sulfur proteins (HiPIPs) is complex: it is not the pattern of a single, isolated S=1/2 system. Multifrequency EPR from 9 to 130 GHz reveals that the apparent peak positions (g values) are frequency-independent: the spectrum is dominated by the Zeeman interaction plus g-strain broadening. The spectra taken at frequencies above the X-band are increasingly sensitive to rapid-passage effects; therefore, the X-band data, which are slightly additionally broadened by dipolar interaction, were used for quantitative spectral analysis. For a single geometrical [4Fe-4S](3+) structure the (Fe-Fe)(5+) mixed-valence dimer can be assigned in six different ways to a pair of iron ions, and this defines six valence isomers. Systematic multicomponent g-strain simulation shows that the [4Fe-4S](3+) paramagnets in seven HiPIPs from different bacteria each consist of three to four discernible species, and these are assigned to valence isomers of the clusters. This interpretation builds on previous EPR analyzes of [4Fe-4S](3+) model compounds, and it constitutes a high-resolution extension of the current literature model, proposed from paramagnetic NMR studies.
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