ArticleJournal of the American Chemical Society2011
Electron transfer reactivity of type zero Pseudomonas aeruginosa azurin.
Article in Journal of the American Chemical Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Article
- Controlling outer-sphere solvent reorganization energy to turn on or off the function of artificial metalloenzymes.Nature communications · 2025Article
- Photoinduced Electron Transfer from the Tryptophan Triplet State in Zn-Azurin.ACS physical chemistry Au · 2023Article
- Role of the Triplet State and Protein Dynamics in the Formation and Stability of the Tryptophan Radical in an Apoazurin Mutant.The journal of physical chemistry. B · 2022Article
- CuChemical science · 2020Article
- Mechanical Deformation and Electronic Structure of a Blue Copper Azurin in a Solid-State Junction.Biomolecules · 2019Article
- Clarifying the Copper Coordination Environment in a de Novo Designed Red Copper Protein.Inorganic chemistry · 2018Article
- The influence of pH and divalent/monovalent cations on the internal electron transfer (IET), enzymatic activity, and structure of fructose dehydrogenase.Analytical and bioanalytical chemistry · 2018Article
- Design of a single protein that spans the entire 2-V range of physiological redox potentials.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Photogeneration and Quenching of Tryptophan Radical in Azurin.The journal of physical chemistry. B · 2015Article
- Tryptophan-to-heme electron transfer in ferrous myoglobins.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Structural studies on Laz, a promiscuous anticancer Neisserial protein.Bioengineered · 2015Article
- Molecular dynamics simulations of apocupredoxins: insights into the formation and stabilization of copper sites under entatic control.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014Article
- Metalloproteins containing cytochrome, iron-sulfur, or copper redox centers.Chemical reviews · 2014Review
- Protein design: toward functional metalloenzymes.Chemical reviews · 2014Review
- Tryptophan-accelerated electron flow across a protein-protein interface.Journal of the American Chemical Society · 2013Article
- Designed azurins show lower reorganization free energies for intraprotein electron transfer.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Catalysis of dioxygen reduction by Thermus thermophilus strain HB27 laccase on ketjen black electrodes.The journal of physical chemistry. B · 2013Article
- Inner- and outer-sphere metal coordination in blue copper proteins.Journal of inorganic biochemistry · 2012Review
- Flexibility of the metal-binding region in apo-cupredoxins.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
Type zero copper is a hard-ligand analogue of the classical type 1 or blue site in copper proteins that function as electron transfer (ET) agents in photosynthesis and other biological processes. The EPR spectroscopic features of type zero Cu(II) are very similar to those of blue copper, although lacking the deep blue color, due to the absence of thiolate ligation. We have measured the rates of intramolecular ET from the pulse radiolytically generated C3-C26 disulfide radical anion to the Cu(II) in both type zero C112D/M121L and type 2 C112D Pseudomonas aeruginosa azurins in pH 7.0 aqueous solutions between 8 and 45 °C. We also have obtained rate/temperature (10-30 °C) profiles for ET reactions between these mutants and the wild-type azurin. Analysis of the rates and activation parameters for both intramolecular and intermolecular ET reactions indicates that the type zero copper reorganization energy falls in a range (0.9-1.1 eV) slightly above that for type 1 (0.7-0.8 eV), but substantially smaller than that for type 2 (>2 eV), consistent with XAS and EXAFS data that reveal minimal type zero site reorientation during redox cycling.
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Registered trials
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