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?

A Flavin Analogue with Improved Solubility in Organic Solvents.

Redox tuning over almost 1 V in a structurally conserved active site: lessons from Fe-containing superoxide dismutase.

Spectroscopic and computational insights into second-sphere amino-acid tuning of substrate analogue/active-site interactions in iron(III) superoxide dismutase.

Spectroscopic and computational insights into second-sphere amino-acid tuning of substrate analogue/active-site interactions in iron(III) superoxide dismutase.

[Anonymous].  2008.  Spectroscopic and computational insights into second-sphere amino-acid tuning of substrate analogue/active-site interactions in iron(III) superoxide dismutase.. Inorganic chemistry. 47(10):3993-4004.

Spectroscopic and computational investigation of second-sphere contributions to redox tuning in Escherichia coli iron superoxide dismutase.

Spectroscopic and computational investigation of second-sphere contributions to redox tuning in Escherichia coli iron superoxide dismutase.

[Anonymous].  2008.  Spectroscopic and computational investigation of second-sphere contributions to redox tuning in Escherichia coli iron superoxide dismutase.. Inorganic chemistry. 47(10):3978-92.