References Cited in Superoxide Dismutase Highlights

Numbering is that of the CV (Download).

16. D. L. Sorkin and A.-F. Miller (1997) "Observation of a Long-Predicted Active Site pK in Fe-Superoxide Dismutase from E. coli." Biochemistry 36(16) 4916-4924. (on-line)
doi: 10.1021/bi963047z

36. C. K. Vance and A.-F. Miller (2001) "Novel Insights into the Basis for E. coli SOD's Metal Ion Specificity, from Mn-Substituted Fe-SOD and its Very High Em." Biochemistry 40: 13079-13087. (on-line)
doi: 10.1021/bi0113317

42. J. Maliekal, A. Karapetian, C. K. Vance, E. Yikilmaz, Q. Wu, T. A. Jackson, T. C. Brunold, T. G. Spiro and A.-F. Miller. (2002) "Comparison and Contrasts Between the Active Site pKs of Mn-Superoxide Dismutase and those of Fe-Superoxide Dismutase." J. Am. Chem. Soc. 124: 15064-15075. (on-line)
doi: 10.1021/ja027319z

49. A.-F. Miller (2004) "Superoxide Dismutase, an Active Site that Saves but a Protein that Kills" Curr. Op. Chem. Biol. 8:162-168. (on-line)
doi: 10.1016/j.cbpa.2004.02.011

52. A.-F. Miller, D. L. Sorkin and K. Padmakumar (2005) "The Anion Binding Properties of Reduced and Oxidized Iron-Containing Superoxide Dismutase Reveal no Requirement for Tyrosine 34." Biochemistry 44(16): 5969-5981. (on-line)
doi: 10.1021/bi0476331

53. E. Yikilmaz, D. W. Rodgers and A.-F. Miller (2006) "The Crucial Importance of Chemistry in the Structure-Function Link: Manipulating H-Bonding in Fe-Superoxide Dismutase." Biochemistry 45(4):1151-1161. (on-line)
doi: 10.1021/bi051495d

57. E. Yikilmaz, J. Porta, L. Grove, A. Vahedi-Faridi, Y. Bronshteyn, T. C. Brunold, G. E. O. Borgstahl and A.-F. Miller (2007) "How can a single second sphere amino acid change cause a reduction midpoint potential change of hundreds of mV ? " J. Am. Chem. Soc. 129: 9927-9940. (on-line)
doi: 10.1021/ja069224t

59. A.-F. Miller (2008) "Redox tuning over almost 1 V in a structurally-conserved active site: lessons from superoxide dismutase.", Acc. Chem. Res. 41 (4) 501-510. (on-line)
doi: 10.1021/ar700237u

72. A.-F. Miller (2012) "Superoxide dismutases: ancient enzymes and new insights." FEBS Lett. 586(5): 585-595. (on-line)
doi:10.1016/j.febslet.2011.10.048

74. A.-F. Miller (2013) "Superoxide Dismutases" Encyclopedia of Biophysics, G. Roberts, V. Davidson, Ed. pp 2517-2522.

81. Sheng, Y., Abreu, I. A., Cabelli, D. E., Maroney, M. J., Miller, A.-F., Teixeira, M. and Valentine, J. S. (2014) "Superoxide dismutases and superoxide reductases" Chem. Rev. 114:3854-3918. (on-line)
doi: 10.1021/cr4005296

91. Miller, A.-F. and Wang, T. (2017) "A single outer-sphere mutation stabilizes apo-Mn superoxide dismutase by 35oC and disfavours Mn binding." Biochemistry 56(29):3787-3799. (on-line)
doi: 10.1021/acs.biochem.7b00175



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