Spectral hole burning and selection of conformational substates in chromoproteins

J. Friedrich, J. Gafert, J. Zollfrank, J. Vanderkooi, J. Fidy

Research output: Contribution to journalArticle

33 Citations (Scopus)


We investigated spectral holes burnt at 1.5 K into the origins of several tautomeric forms of mesoporphyrin IX-substituted horseradish peroxidase at pH 8 under pressures up to 2 MPa. From the pressure-induced lineshift the compressibility of the apoprotein could be determined. We found that the compressibility changed significantly when measured at different tautomer origins. It was concluded that there must be a correlation between the tautomer configurations of the chromophore and the actual structures of the apoprotein. As a consequence, specific conformational substates of the protein can be selected by optical selection of the associated tautomers.

Original languageEnglish
Pages (from-to)1029-1033
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number3
Publication statusPublished - Feb 1 1994


  • compressibility
  • disorder phenomena
  • horseradish peroxidase

ASJC Scopus subject areas

  • General

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