Mutation of tyrosine 34 to phenylalanine eliminates the active site pK of reduced iron-containing superoxide dismutase.

doi:10.1021/bi970533t

Back to search

Article

Mutation of tyrosine 34 to phenylalanine eliminates the active site pK of reduced iron-containing superoxide dismutase.

Biochemistry - 8 Jul 1997

Sorkin D L, Duong D K, Miller A F

Abstract excerpt

We have compared the magnetic resonance properties and pH dependence of wild-type and mutant Fe-containing superoxide dismutase (Fe-SOD) in which the conserved active site tyrosine (Tyr 34) is replaced by phenylalanine. The EPR spectrum of the oxidized state and the NMR spectrum of the paramagnet...

Topics

Binding Sites
Electrochemistry
Electron Spin Resonance Spectroscopy
Hydrogen Bonding
Hydrogen-Ion Concentration
Hydroxyl Radical
Iron
Magnetic Resonance Spectroscopy
Mutation
Oxidation-Reduction
Phenylalanine
Superoxide Dismutase
Tyrosine

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.