By the same authors

From the same journal

FLUORESCENCE PROPERTIES OF SUBTILISINS AND RELATED PROTEINASES (SUBTILASES): RELATION TO X-RAY MODELS

Research output: Contribution to journalArticle

Author(s)

  • N GENOV
  • P NICOLOV
  • C BETZEL
  • K WILSON
  • P DOLASHKA

Department/unit(s)

Publication details

JournalJOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY B-BIOLOGY
DatePublished - May 1993
Issue number2-3
Volume18
Number of pages8
Pages (from-to)265-272
Original languageEnglish

Abstract

The fluorescence properties of six subtilases with known X-ray structure were determined using the same experimental conditions and instrumentation. The steady state and nanosecond lifetime measurements were performed on purified samples of phenylmethanesulphonyl-inhibited proteinases in the presence of 20 mM CaCl2 which stabilizes the molecules. The tryptophan emission quantum yield strongly depends on the local environment and varies from 0.02 to 0.10. The efficiency of tyrosine-to-tryptophan energy transfer also varies (O%-70%) in the different enzymes; the most efficient transfer was observed for thermitase.

Experiments with nanosecond excitation indicated that the tryptophan fluorescence of subtilases decays with two exponential components. The X-ray models of the six proteinases were analysed in the region of the tryptophyl residues and were used to explain the observed properties.

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