ArticleJournal of the American Chemical Society2012
Outer-sphere contributions to the electronic structure of type zero copper proteins.
Article in Journal of the American Chemical Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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12 citing papers in PubMed, 41 citations in OpenAlex.
- Analysis of a Cu-Doped Metal-Organic Framework, MFM-520(ZnAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Converged Structural and Spectroscopic Properties for Refined QM/MM Models of Azurin.Inorganic chemistry · 2021Article
- Trinuclear copper biocatalytic center forms an active site of thiocyanate dehydrogenase.Proceedings of the National Academy of Sciences of the United States of America · 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
- Accurate Quantum Mechanical/Molecular Mechanical Calculations of Reduction Potentials in Azurin Variants.Journal of chemical theory and computation · 2018Article
- Engineering a bifunctional copper site in the cupredoxin fold by loop-directed mutagenesis.Chemical science · 2018Article
- Modular Artificial Cupredoxins.Journal of the American Chemical Society · 2016Article
- Reversible S-nitrosylation in an engineered azurin.Nature chemistry · 2016Article
- 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
- Inner- and outer-sphere metal coordination in blue copper proteins.Journal of inorganic biochemistry · 2012Review
- Spin delocalization over type zero copper.Inorganic chemistry · 2012Article
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Authors and funding
9 authors at 6 institutions in 5 countries.
Funding
Abstract
Bioinorganic canon states that active-site thiolate coordination promotes rapid electron transfer (ET) to and from type 1 copper proteins. In recent work, we have found that copper ET sites in proteins also can be constructed without thiolate ligation (called "type zero" sites). Here we report multifrequency electron paramagnetic resonance (EPR), magnetic circular dichroism (MCD), and nuclear magnetic resonance (NMR) spectroscopic data together with density functional theory (DFT) and spectroscopy-oriented configuration interaction (SORCI) calculations for type zero Pseudomonas aeruginosa azurin variants. Wild-type (type 1) and type zero copper centers experience virtually identical ligand fields. Moreover, O-donor covalency is enhanced in type zero centers relative that in the C112D (type 2) protein. At the same time, N-donor covalency is reduced in a similar fashion to type 1 centers. QM/MM and SORCI calculations show that the electronic structures of type zero and type 2 are intimately linked to the orientation and coordination mode of the carboxylate ligand, which in turn is influenced by outer-sphere hydrogen bonding.
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