ArticleJournal of the American Chemical Society2010
Outer-sphere effects on reduction potentials of copper sites in proteins: the curious case of high potential type 2 C112D/M121E Pseudomonas aeruginosa azurin.
Article in Journal of the American Chemical Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
11 citing papers in PubMed, 34 citations in OpenAlex.
- Designing Artificial Metalloenzymes by Tuning of the Environment beyond the Primary Coordination Sphere.Chemical reviews · 2022Review
- Frustration Dynamics and Electron-Transfer Reorganization Energies in Wild-Type and Mutant Azurins.Journal of the American Chemical Society · 2022Article
- Traversing the Red-Green-Blue Color Spectrum in Rationally Designed Cupredoxins.Journal of the American Chemical Society · 2020Article
- Controlling a burn: outer-sphere gating of hydroxylamine oxidation by a distal base in cytochrome P460.Chemical science · 2019Article
- Design and fine-tuning redox potentials of metalloproteins involved in electron transfer in bioenergetics.Biochimica et biophysica acta · 2016Review
- Metalloproteins containing cytochrome, iron-sulfur, or copper redox centers.Chemical reviews · 2014Review
- Protein design: toward functional metalloenzymes.Chemical reviews · 2014Review
- A Euclidean Perspective on the Unfolding of Azurin: Spatial Correlations.Molecular physics · 2013Article
- Azurin as a protein scaffold for a low-coordinate nonheme iron site with a small-molecule binding pocket.Journal of the American Chemical Society · 2012Article
- Flexibility of the metal-binding region in apo-cupredoxins.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Electron transfer reactivity of type zero Pseudomonas aeruginosa azurin.Journal of the American Chemical Society · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Redox and spectroscopic (electronic absorption, multifrequency electron paramagnetic resonance (EPR), and X-ray absorption) properties together with X-ray crystal structures are reported for the type 2 Cu(II) C112D/M121E variant of Pseudomonas aeruginosa azurin. The results suggest that Cu(II) is constrained from interaction with the proximal glutamate; this structural frustration implies a "rack" mechanism for the 290 mV (vs NHE) reduction potential measured at neutral pH. At high pH (∼9), hydrogen bonding in the outer coordination sphere is perturbed to allow axial glutamate ligation to Cu(II), with a decrease in potential to 119 mV. These results highlight the role played by outer-sphere interactions, and the structural constraints they impose, in determining the redox behavior of transition metal protein cofactors.
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What OpenQuestion holds
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.