ArticleInorganic chemistry2015
Characterization of the Copper(II) Binding Sites in Human Carbonic Anhydrase II.
Article in Inorganic chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 26 citations in OpenAlex.
- Structural insights into copper and zinc binding to tau protein and the impact of metal binding on amyloid aggregation.Chemical science · 2026Article
- Energetics and dynamics of the proton shuttle of carbonic anhydrase II.Cellular and molecular life sciences : CMLS · 2023Article
- Synthesis, characterization and biological evaluation of pyrazole-based benzene sulfonamides as inhibitors of human carbonic anhydrase II, IX and XII.RSC advances · 2023Article
- Metal Ion Binding Induces Local Protein Unfolding and Destabilizes Human Carbonic Anhydrase II.Inorganic chemistry · 2022Article
- Reconsidering anion inhibitors in the general context of drug design studies of modulators of activity of the classical enzyme carbonic anhydrase.Journal of enzyme inhibition and medicinal chemistry · 2021Review
- Review
- Article
- Carbonic anhydrase modification for carbon management.Environmental science and pollution research international · 2020Article
- Pull-Down of Metalloproteins in Their Native States by Using Desthiobiotin-Based Probes.Chembiochem : a European journal of chemical biology · 2019Article
- Dioxygen, an unexpected carbonic anhydrase ligand.Journal of enzyme inhibition and medicinal chemistry · 2018Article
- Article
- Long-range paramagnetic NMR data can provide a closer look on metal coordination in metalloproteins.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Article
- Global stability of an α-ketoglutarate-dependent dioxygenase (TauD) and its related complexes.Biochimica et biophysica acta. General subjects · 2017Article
- Coordination contributions to protein stability in metal-substituted carbonic anhydrase.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2016Article
- The Complex Relationship between Metals and Carbonic Anhydrase: New Insights and Perspectives.International journal of molecular sciences · 2016Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Human carbonic anhydrase (CA) is a well-studied, robust, mononuclear Zn-containing metalloprotein that serves as an excellent biological ligand system to study the thermodynamics associated with metal ion coordination chemistry in aqueous solution. The apo form of human carbonic anhydrase II (CA) binds 2 equiv of copper(II) with high affinity. The Cu(2+) ions bind independently forming two noncoupled type II copper centers in CA (CuA and CuB). However, the location and coordination mode of the CuA site in solution is unclear, compared to the CuB site that has been well-characterized. Using paramagnetic NMR techniques and X-ray absorption spectroscopy we identified an N-terminal Cu(2+) binding location and collected information on the coordination mode of the CuA site in CA, which is consistent with a four- to five-coordinate N-terminal Cu(2+) binding site reminiscent to a number of N-terminal copper(II) binding sites including the copper(II)-amino terminal Cu(2+) and Ni(2+) and copper(II)-β-amyloid complexes. Additionally, we report a more detailed analysis of the thermodynamics associated with copper(II) binding to CA. Although we are still unable to fully deconvolute Cu(2+) binding data to the high-affinity CuA site, we derived pH- and buffer-independent values for the thermodynamics parameters K and ΔH associated with Cu(2+) binding to the CuB site of CA to be 2 × 10(9) and -17.4 kcal/mol, respectively.
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