Horseradish peroxidase monitored by infrared spectroscopy: Effect of temperature, substrate and calcium

A. Kaposi, J. Fidy, Eric S. Manas, Jane M. Vanderkooi, Wayne W. Wright

Research output: Contribution to journalArticle

32 Citations (Scopus)

Abstract

Horseradish peroxidase was examined as a function of Ca and substrate binding using infrared spectroscopy in the temperature range of 10-300 K. The Ca complex could be identified by the carboxylate stretches. The amide peak positions indicate that the protein remains stable from room temperature to 10 K. Shifts in these peaks are consistent with increased hydrogen bonding as temperature decreases, but the protein conformation is maintained at cryogenic temperatures. The substrate, benzohydroxamic acid, produced no detectable change in the infrared spectrum, consistent with X-ray crystallography results. With removal of Ca, the protein maintained its overall helicity.

Original languageEnglish
Pages (from-to)41-50
Number of pages10
JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Volume1435
Issue number1-2
DOIs
Publication statusPublished - Nov 16 1999

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Horseradish Peroxidase
Infrared spectroscopy
Spectrum Analysis
Calcium
Temperature
Substrates
Protein Conformation
Proteins
X ray crystallography
X Ray Crystallography
Hydrogen Bonding
Amides
Cryogenics
Conformations
Hydrogen bonds
Infrared radiation

Keywords

  • Alpha helix
  • Benzohydroxamic acid
  • Hydrogen bonding

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Structural Biology
  • Biophysics

Cite this

Horseradish peroxidase monitored by infrared spectroscopy : Effect of temperature, substrate and calcium. / Kaposi, A.; Fidy, J.; Manas, Eric S.; Vanderkooi, Jane M.; Wright, Wayne W.

In: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular, Vol. 1435, No. 1-2, 16.11.1999, p. 41-50.

Research output: Contribution to journalArticle

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