Lack of correspondence between the room-temperature phosphorescence decay-components and Trp residues in a series of Trp-->Cys or Trp-->Phe mutants of human carbonic anhydrase II.

doi:10.1016/0014-5793(94)01041-2

Article

Lack of correspondence between the room-temperature phosphorescence decay-components and Trp residues in a series of Trp-->Cys or Trp-->Phe mutants of human carbonic anhydrase II.

FEBS letters - 17 Oct 1994

Bergenhem N C, Schlyer B D, Steel D G, Gafni A, Carlsson U, Jonsson B H

Abstract excerpt

The room temperature phosphorescence of native human carbonic anhydrase (CA), and several mutants of this enzyme has been investigated. In these mutants the seven tryptophan residues in the native protein have sequentially been replaced by cysteine or phenylalanine. All of the mutants as well as...

Topics

Carbonic Anhydrases
Chemical Phenomena
Chemistry, Physical
Cysteine
Humans
Kinetics
Luminescence
Mutation
Phenylalanine
Spectrophotometry
Temperature
Tryptophan

Lack of correspondence between the room-temperature phosphorescence decay-components and Trp residues in a series of Trp-->Cys or Trp-->Phe mutants of human carbonic anhydrase II.

Abstract excerpt

Topics

Discuss the evidence