ArticleBiophysical journal2008
Electron-electron distances in spin-labeled low-spin metmyoglobin variants by relaxation enhancement.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed, 18 citations in OpenAlex.
- Unexpected Heme Redox Potential Values Implicate an Uphill Step in CytochromeThe journal of physical chemistry. B · 2022Article
- Article
- Distinct properties of semiquinone species detected at the ubiquinol oxidation Qo site of cytochrome bc1 and their mechanistic implications.Journal of the Royal Society, Interface · 2016Review
- Long-range distance measurements in proteins at physiological temperatures using saturation recovery EPR spectroscopy.Journal of the American Chemical Society · 2014Article
- Molecular organization of cytochrome c2 near the binding domain of cytochrome bc1 studied by electron spin-lattice relaxation enhancement.The journal of physical chemistry. B · 2014Article
- A caged, destabilized, free radical intermediate in the q-cycle.Chembiochem : a European journal of chemical biology · 2013Article
- EPR relaxation-enhancement-based distance measurements on orthogonally spin-labeled T4-lysozyme.Chembiochem : a European journal of chemical biology · 2013Article
- Magnetic interactions sense changes in distance between heme b(L) and the iron-sulfur cluster in cytochrome bc(1).Biochemistry · 2009Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Thirteen single-cysteine variants of myoglobin were prepared by overexpression of apoprotein, spin labeling, and reconstitution with hemin. This procedure resulted in a protein with fewer hemichrome impurities than was obtained by an overexpression of holo-protein followed by spin labeling. Coordination of cyanide to the met heme formed low-spin complexes. Iron-nitroxyl interspin distances in the range of 17-30 A were determined by saturation recovery measurements of the enhancement of the nitroxyl spin lattice relaxation rates between approximately 30-140 K, and by spin-echo measurements of the enhancement of spin-spin relaxation rates at 10-30 K. Interspin distances were also calculated, using the molecular modeling program Insight II (Accelrys, San Diego, CA). For most variants, distances determined from the temperature dependence of spin-echo intensities at a pulse spacing of 200 ns agree with distances measured by saturation recovery and calculated with Insight II within about an angstrom, which is within experimental uncertainties. Measurements of interspin distances via spin-spin relaxation enhancement have the advantages that maximum effects are observed for slower metal relaxation rates than are required for spin-lattice relaxation enhancement, and the impact diminishes as r(-3) instead of r(-6), as with spin-lattice relaxation enhancement, which permits measurements at longer distances.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.