ArticleProtein science : a publication of the Protein Society2017
Effect of circular permutation on the structure and function of type 1 blue copper center in azurin.
Article in Protein science : a publication of the Protein Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 15 citations in OpenAlex.
- Structural basis for organism-dependent effects on spectroscopic properties of type 1 copper azurin by the same axial methionine to histidine mutation.Journal of inorganic biochemistry · 2026Article
- Circular permutation at azurin's active site slows down its folding.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2023Article
- CuChemical science · 2020Article
- Two Tryptophans Are Better Than One in Accelerating Electron Flow through a Protein.ACS central science · 2019Article
- Investigating the Effect of Chain Connectivity on the Folding of a Beta-Sheet Protein On and Off the Ribosome.Journal of molecular biology · 2018Article
- Clarifying the Copper Coordination Environment in a de Novo Designed Red Copper Protein.Inorganic chemistry · 2018Article
Corrections and comments
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Authors and funding
7 authors at 5 institutions in 2 countries.
Funding
Abstract
Type 1 copper (T1Cu) proteins are electron transfer (ET) proteins involved in many important biological processes. While the effects of changing primary and secondary coordination spheres in the T1Cu ET function have been extensively studied, few report has explored the effect of the overall protein structural perturbation on active site configuration or reduction potential of the protein, even though the protein scaffold has been proposed to play a critical role in enforcing the entatic or "rack-induced" state for ET functions. We herein report circular permutation of azurin by linking the N- and C-termini and creating new termini in the loops between 1
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