FTIR studies of organometalcarbonyl-tagged enzymes

Christopher E. Anson, Colin S. Creaser, Orsolya Egyed, G. Richard Stephenson

Research output: Contribution to journalArticle

20 Citations (Scopus)

Abstract

Attachment of organometaltricarbonyl tags to enzymes is revealed by changes in the vibrational modes of the carbonyl groups. Shoulders on νsym(CO) and νasym(CO) bands in the FTIR spectrum of an organometallic tag derived from tricarbonyl[1-{(2,3,4,5-η)-2,4-cyclohexadien-1-yl}pyridinium]iron(1 + ) hexafluorophosphate(1 - ) were detected on binding to enzymes (α-chymotrypsin, ribonuclease A, alkaline phosphatase and a triacylglycerol lipase). By comparison with tagging reactions between the tricarbonyliron moiety and model compounds, the new spectral features were attributed to an iron complex covalently bonded to the NH2 groups of the amino acid residues of the enzymes. FTIR spectroscopy was used to monitor deprotonation of tagged amino groups on the enzyme surface. Interactions between the organometalcarbonyl tag and other side-chain groups of the amino acid residues were also investigated.

Original languageEnglish
Pages (from-to)1867-1877
Number of pages11
JournalSpectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy
Volume53
Issue number11
DOIs
Publication statusPublished - Oct 1 1997

Keywords

  • Infrared spectroscopy
  • Organometallic label
  • Proteins
  • Spectroscopic probe

ASJC Scopus subject areas

  • Analytical Chemistry
  • Atomic and Molecular Physics, and Optics
  • Instrumentation
  • Spectroscopy

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