Azurin

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Azurin is a bacterial blue copper protein found in Pseudomonas, Bordetella, or Alcaligenes bacteria, which undergoes oxidation-reduction between Cu(I) and Cu(II), and transfers single electrons between enzymes associated with the cytochrome chain. The protein has a molecular weight of approximately 16,000, contains a single copper atom, is intensively blue, and has a fluorescence emission band centered at 308 nm.

Azurins and pseudoazurins participate in denitrification processes in bacteria.[1]

Azurin and cytochrome c551 are involved in electron transfer during denitrification in P. aeruginosa. Azurin from P aeruginosa is a type I blue copper protein with a molecular mass of 14 kDa, while cytochrome c551 (9 kDa) is a haem-containing cytochrome. Azurin possesses a relatively large hydrophobic patch close to the active site, and two residues in this hydrophobic patch, Met-44 and Met-64, are believed to be involved in its interaction with the redox partners cytochrome c551 and nitrite reductase[2]

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  1. ^ De Rienzo F, Gabdoulline RR, Menziani MC, Wade RC (2000). "Blue copper proteins: a comparative analysis of their molecular interaction properties.". Protein Sci. 9 (8): 1439–54. PMC 2144732Freely accessible. PMID 10975566. doi:10.1110/ps.9.8.1439. 
  2. ^ Tohru Yamada; Masatoshi Goto; Vasu Punj; Olga Zaborina; Kazuhide Kimbara; T. K. Das Gupta & A. M. Chakrabarty (Dec 2002). "The Bacterial Redox Protein Azurin Induces Apoptosis in J774 Macrophages through Complex Formation and Stabilization of the Tumor Suppressor Protein p53". Infect Immun. 70 (12): 7054–7062. PMC 133031Freely accessible. PMID 12438386. doi:10.1128/IAI.70.12.7054-7062.2002.