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Lack of correspondence between the room‐temperature phosphorescence decay‐components and Trp residues in a series of Trp→Cys or Trp→Phemutants of human carbonic anhydrase II
Author(s) -
Bergenhem Nils C.H.,
Schlyer Bruce D.,
Steel Duncan G.,
Gafni Ari,
Carlsson Uno,
Jonsson Bengt-Harald
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)01041-2
Subject(s) - phosphorescence , tryptophan , chemistry , carbonic anhydrase ii , residue (chemistry) , cysteine , mutant , kinetics , carbonic anhydrase , enzyme , phenylalanine , photochemistry , biochemistry , stereochemistry , fluorescence , amino acid , physics , quantum mechanics , gene
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 In these mutants the seven tryptophan residues in the native protein have sequentially been replaced by cysteine or phenylalanine.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 native CA show room‐temperature tryptophan phosphorescence (RTP) spectra. Surprisingly, only small differences in RTP life‐times are noticeable among these mutants, indicating that there is more than one tryptophan residue with similar phosphorescence decay kinetics in the protein. The present results illustrate the danger in attributing the room temperature phosphorescence of a multi‐tryptophan protein to a particular residue based solely on an analysis of the protein structure.