ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2011
Incorporation of the red copper nitrosocyanin binding loop into blue copper azurin.
Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2011. 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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6 citing papers in PubMed, 20 citations in OpenAlex.
- Beyond the coupled distortion model: structural analysis of the single domain cupredoxin AcoP, a green mononuclear copper centre with original features.Dalton transactions (Cambridge, England : 2003) · 2024Article
- CuChemical science · 2020Article
- Effect of circular permutation on the structure and function of type 1 blue copper center in azurin.Protein science : a publication of the Protein Society · 2017Article
- Metalloproteins containing cytochrome, iron-sulfur, or copper redox centers.Chemical reviews · 2014Review
- Protein design: toward functional metalloenzymes.Chemical reviews · 2014Review
- Dynamics and unfolding pathway of chimeric azurin variants: insights from molecular dynamics simulation.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2013Article
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4 authors at 1 institution in 1 country.
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Abstract
Loop-directed mutagenesis was applied to the blue copper protein azurin to replace its copper binding loop with that from the red copper protein nitrosocyanin. A ten amino acid long loop that provides three of the four copper ligands from nitrosocyanin was incorporated into azurin to make a variant called NC-azurin. The chimeric protein displayed a red color, and UV-vis absorption and EPR spectra that closely resembled those of the loop parent, nitrosocyanin. We added the fourth ligand from nitrosocyanin into NC-azurin, a carboxylate-containing amino acid, but the proteins had altered stability and spectroscopic properties that did not resemble those of either parent copper protein. The loop alone, however, was enough to impart red copper site characteristics to the NC-azurin protein. Finally, the reduction potential of the variant was found to be between the reduction potentials of the parent proteins and about 50 mV below that of wild-type azurin.
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