OHSU

Ninian Blackburn

Ninian Blackburn

Email:
Phone: 503 748-1384
Fax: 503 748-1464
Lab Phone: 503 748-1086

 

Current Appointments

Professor, Department of Environmental and Biomolecular Systems

 

Education

Ph.D., Inorganic Chemistry; University of Dundee, Scotland, U.K., 1975

 

Biography

  • Postdoctoral studies in biophysical chemistry with Howard S. Mason at the
    Oregon Health Sciences University and Peter F. Knowles at Leeds, 1974-79
  • Lecturer in Inorganic Chemistry, University of Manchester Institute
    of Science and Technology, 1979-87
  • Visiting Lecturer, University of Sydney, 1987

 

Research Interests

Structure and function of oxidase and oxygenase metalloenzymes; spectroscopy of metal sites in proteins with emphasis on EPR, EXAFS, absorption edge, and FTIR spectroscopies; coordination chemistry and biochemistry of copper. Biochemistry of metal trafficking in cells.

 

Selected Publications

Otoikhian, A.; Barry, A. N.; Mayfield, M.; Nilges, M.; Huang, Y.; Lutsenko, S.; Blackburn, N. J. (2012) Lumenal loop M672-P707 of the Menkes protein (ATP7A) transfers copper to peptidylglycine monooxygenase. J. Am. Chem. Soc., 134, 10458-10468. (DOI: 10.1021/ja301221s)

Mealman, T. D.; Zhou, M.; Affandi, T.; Chacon, K. N.; Aranguren, M. E.; Blackburn, N. J.; Wysocki, V. H.; McEvoy, M. M. (2012) N-Terminal region of CusB Is sufficient for metal binding and metal transfer with the metallochaperone CusF. Biochemistry, 51, 6767-6775. (DOI: 10.1021/bi300596a)

Mealman, T. D.; Blackburn, N. J.; McEvoy, M. M. (2012) Metal export by CusCFBA, the periplasmic Cu(I)/Ag(I) transport system of Escherichia coli. Curr. Top. Membr., 69, 163-196.

Chacon, K. N.; Blackburn, N. J. (2012) Stable Cu(II) and Cu(I) mononuclear intermediates in the assembly of the CuA center of Thermus thermophilus cytochrome oxidase. J. Am. Chem. Soc., 134, 16401-16412. (DOI: 10.1021/ja307276z)

Abriata, L. A.; Alvarez-Paggi, D.; Ledesma, G. N.; Blackburn, N. J.; Vila, A. J.; Murgida, D. H. (2012) Alternative ground states enable pathway switching in biological electron transfer. Proc. Natl. Acad. Sci. U. S. A., Early Ed., 1-6, 6 pp. (DOI: 10.1073/pnas.1204251109)

Siluvai, G. S.; Nakano, M.; Mayfield, M.; Blackburn, N. J. (2011) The essential role of the Cu(II) state of Sco in the maturation of the CuA center of cytochrome oxidase: evidence from H135Met and H135SeM variants of the Bacillus subtilis Sco. J. Biol. Inorg. Chem., 16, 285-297. (DOI: 10.1007/s00775-010-0725-z)

Bauman, A. T.; Broers, B. A.; Kline, C. D.; Blackburn, N. J. (2011) A copper-methionine interaction controls the pH-dependent activation of peptidylglycine monooxygenase. Biochemistry, 50, 10819-10828. (DOI: 10.1021/bi201193j)

Barry, A. N.; Otoikhian, A.; Bhatt, S.; Shinde, U.; Tsivkovskii, R.; Blackburn, N. J.; Lutsenko, S. (2011) The lumenal loop Met672-Pro707 of Copper-transporting ATPase ATP7A binds metals and facilitates copper release from the intramembrane sites. J. Biol. Chem., 286, 26585-26594, S26585/26581-S26585/26587. (DOI: 10.1074/jbc.M111.229039)

Siluvai, G. S.; Mayfield, M.; Nilges, M. J.; De, B. G. S.; Blackburn, N. J. (2010) Anatomy of a red copper center: Spectroscopic identification and reactivity of the copper centers of Bacillus subtilis Sco and its Cys-to-Ala variants. J. Am. Chem. Soc., 132, 5215-5226. (DOI: 10.1021/ja910759v)

Le, S. E. S.; Shinde, U.; Walker, J. M.; Barry, A. N.; Blackburn, N. J.; Ralle, M.; Lutsenko, S. (2010) Interactions between copper-binding sites determine the redox status and conformation of the regulatory N-terminal domain of ATP7B. J. Biol. Chem., 285, 6327-6336. (DOI: 10.1074/jbc.M109.074633)

Hess, C. R.; Klinman, J. P.; Blackburn, N. J. (2010) The copper centers of tyramine B-monooxygenase and its catalytic-site methionine variants: an x-ray absorption study. J. Biol. Inorg. Chem., 15, 1195-1207. (DOI: 10.1007/s00775-010-0677-3)

Clark, K. M.; Yu, Y.; Marshall, N. M.; Sieracki, N. A.; Nilges, M. J.; Blackburn, N. J.; van, d. D. W. A.; Lu, Y. (2010) Transforming a blue copper into a red copper protein: Engineering cysteine and homocysteine into the axial position of azurin using site-directed mutagenesis and expressed protein ligation. J. Am. Chem. Soc., 132, 10093-10101. (DOI: 10.1021/ja102632p)

Blackburn, N. J. (2010) A tale of two metals. Chem. Biol. (Cambridge, MA, U. S.), 17, 8-9. (DOI: 10.1016/j.chembiol.2010.01.004)