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1. Effect of circular permutation on the structure and function of type 1 blue copper center in azurin: Circular Permutation Effect on T1Cu in Azurin

   https://doi.org/10.1002/pro.3071  

   Yu, Yang ; Petrik, Igor D. ; Chacón, Kelly N. ; Hosseinzadeh, Parisa ; Chen, Honghui ; Blackburn, Ninian J. ; Lu, Yi ( February 2017 , Protein Science)
2. Sequence-specific destabilization of azurin by tetramethylguanidinium-dipeptide ionic liquids

   https://doi.org/10.1016/j.bbrep.2022.101242  

   Patel, Roshani ; Clark, Austin K. ; DeStefano, Gabriella ; DeStefano, Isabella ; Gogoj, Hunter ; Gray, Erin ; Patel, Aashka Y. ; Hauner, Joshua T. ; Caputo, Gregory A. ; Vaden, Timothy D. ( July 2022 , Biochemistry and Biophysics Reports)
3. Binuclear Cu A Formation in Biosynthetic Models of Cu A in Azurin Proceeds via a Novel Cu(Cys) 2 His Mononuclear Copper Intermediate

   https://doi.org/10.1021/acs.biochem.5b00659  

   Chakraborty, Saumen ; Polen, Michael J. ; Chacón, Kelly N. ; Wilson, Tiffany D. ; Yu, Yang ; Reed, Julian ; Nilges, Mark J. ; Blackburn, Ninian J. ; Lu, Yi ( October 2015 , Biochemistry)
4. Stepwise nitrosylation of the nonheme iron site in an engineered azurin and a molecular basis for nitric oxide signaling mediated by nonheme iron proteins

   https://doi.org/10.1039/d1sc00364j  

   Tian, Shiliang ; Fan, Ruixi ; Albert, Therese ; Khade, Rahul L. ; Dai, Huiguang ; Harnden, Kevin A. ; Hosseinzadeh, Parisa ; Liu, Jing ; Nilges, Mark J. ; Zhang, Yong ; et al ( May 2021 , Chemical Science)

   null (Ed.)

   Mononitrosyl and dinitrosyl iron species, such as {FeNO} 7 , {FeNO} 8 and {Fe(NO) 2 } 9 , have been proposed to play pivotal roles in the nitrosylation processes of nonheme iron centers in biological systems. Despite their importance, it has been difficult to capture and characterize them in the same scaffold of either native enzymes or their synthetic analogs due to the distinct structural requirements of the three species, using redox reagents compatible with biomolecules under physiological conditions. Here, we report the realization of stepwise nitrosylation of a mononuclear nonheme iron site in an engineered azurin under such conditions. Through tuning the number of nitric oxide equivalents and reaction time, controlled formation of {FeNO} 7 and {Fe(NO) 2 } 9 species was achieved, and the elusive {FeNO} 8 species was inferred by EPR spectroscopy and observed by Mössbauer spectroscopy, with complemental evidence for the conversion of {FeNO} 7 to {Fe(NO) 2 } 9 species by UV-Vis, resonance Raman and FT-IR spectroscopies. The entire pathway of the nitrosylation process, Fe( ii ) → {FeNO} 7 → {FeNO} 8 → {Fe(NO) 2 } 9 , has been elucidated within the same protein scaffold based on spectroscopic characterization and DFT calculations. These results not only enhance the understanding of the dinitrosyl iron complex formation process, but also shed light on the physiological roles of nitric oxide signaling mediated by nonheme iron proteins. 

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5. Tuning reduction potentials of type 1 copper center in azurin by replacing a histidine ligand with its isostructural analogues

   https://doi.org/10.1016/j.jinorgbio.2022.111863  

   Yu, Yang ; Marshall, Nicholas M. ; Garner, Dewain K. ; Nilges, Mark J. ; Lu, Yi ( September 2022 , Journal of Inorganic Biochemistry)