Proton-coupled electron transfer in Fe-superoxide dismutase and Mn-superoxide dismutase.

Spectroscopic and computational study of a non-heme iron Fe-NO 7 system: exploring the geometric and electronic structures of the nitrosyl adduct of iron superoxide dismutase.

Spectroscopic and computational study of a non-heme iron Fe-NO 7 system: exploring the geometric and electronic structures of the nitrosyl adduct of iron superoxide dismutase.

[Anonymous].  2003.  Spectroscopic and computational study of a non-heme iron Fe-NO 7 system: exploring the geometric and electronic structures of the nitrosyl adduct of iron superoxide dismutase.. Journal of the American Chemical Society. 125(27):8348-63.

Superoxide dismutases: active sites that save, but a protein that kills.

Spectroscopic and computational studies of the azide-adduct of manganese superoxide dismutase: definitive assignment of the ligand responsible for the low-temperature thermochromism.

Spectroscopic and computational studies of the azide-adduct of manganese superoxide dismutase: definitive assignment of the ligand responsible for the low-temperature thermochromism.

[Anonymous].  2004.  Spectroscopic and computational studies of the azide-adduct of manganese superoxide dismutase: definitive assignment of the ligand responsible for the low-temperature thermochromism.. Journal of the American Chemical Society. 126(39):12477-91.

Probing the geometric and electronic structures of the low-temperature azide adduct and the product-inhibited form of oxidized manganese superoxide dismutase.

Probing the geometric and electronic structures of the low-temperature azide adduct and the product-inhibited form of oxidized manganese superoxide dismutase.

[Anonymous].  2005.  Probing the geometric and electronic structures of the low-temperature azide adduct and the product-inhibited form of oxidized manganese superoxide dismutase.. Biochemistry. 44(5):1504-20.

Anion binding properties of reduced and oxidized iron-containing superoxide dismutase reveal no requirement for tyrosine 34.

The crucial importance of chemistry in the structure-function link: manipulating hydrogen bonding in iron-containing superoxide dismutase.

The crucial importance of chemistry in the structure-function link: manipulating hydrogen bonding in iron-containing superoxide dismutase.

[Anonymous].  2006.  The crucial importance of chemistry in the structure-function link: manipulating hydrogen bonding in iron-containing superoxide dismutase.. Biochemistry. 45(4):1151-61.

Evidence for polyproline II helical structure in short polyglutamine tracts.

15N solid-state NMR provides a sensitive probe of oxidized flavin reactive sites.

How can a single second sphere amino acid substitution cause reduction midpoint potential changes of hundreds of millivolts?