Structural changes and internal fields in proteins: A hole-burning stark effect study of horseradish peroxidase

Jürgen Gafert, Josef Friedrich, Jane M. Vanderkooi, J. Fidy

Research output: Contribution to journalArticle

28 Citations (Scopus)

Abstract

We compare the Stark spectra of photochemical holes burnt into a globular chromoprotein, namely mesoporphyrin-substituted horseradish peroxidase, with the respective behavior in a glass sample. From the distinct patterns between glass and protein as well as between various burn frequencies in the protein, we can clearly demonstrate that the chromophore in the protein is decoupled from the host glass and, hence, definitely probes the protein. Moreover, the electric fields in the protein pocket are quite different for the various tautomer states. These characteristic features are linked to allosteric-like behavior of proteins.

Original languageEnglish
Pages (from-to)5223-5227
Number of pages5
JournalJournal of Physical Chemistry
Volume99
Issue number15
Publication statusPublished - 1995

Fingerprint

Stark effect
Staphylococcal Protein A
hole burning
Horseradish Peroxidase
proteins
Proteins
Glass
glass
tautomers
Chromophores
chromophores
Electric fields
electric fields
probes

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry

Cite this

Structural changes and internal fields in proteins : A hole-burning stark effect study of horseradish peroxidase. / Gafert, Jürgen; Friedrich, Josef; Vanderkooi, Jane M.; Fidy, J.

In: Journal of Physical Chemistry, Vol. 99, No. 15, 1995, p. 5223-5227.

Research output: Contribution to journalArticle

Gafert, Jürgen ; Friedrich, Josef ; Vanderkooi, Jane M. ; Fidy, J. / Structural changes and internal fields in proteins : A hole-burning stark effect study of horseradish peroxidase. In: Journal of Physical Chemistry. 1995 ; Vol. 99, No. 15. pp. 5223-5227.
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