Comparison of nitrophenylethyl and hydroxyphenacyl caging groups

Biopolymers. 2001;62(3):147-9. doi: 10.1002/bip.1007.

Abstract

Nitrophenylethyl (NPE)- and hydroxyphenacyl (HPA)-caged nucleotides were employed in a time-resolved Fourier transform IR spectroscopy study on Ras-catalyzed guanosine triphosphate (GTP) hydrolysis. A fast kinetic component was observed following the photolysis of NPE-caged nucleotides in the NPE-GTP-Ras complex. However, this kinetic component was not observed in the HPA-GTP-Ras experiment. This fast kinetic component was likely due to a chemical reaction between Ras and the detached caging group, nitrosoacetophenone. This communication serves as a note of caution in interpreting spectral changes and kinetic behavior of the enzymatic systems employing NPE-caged compounds.

Publication types

  • Comparative Study
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Guanosine Triphosphate / analogs & derivatives
  • Guanosine Triphosphate / chemistry*
  • Hydrolysis
  • In Vitro Techniques
  • Nitroso Compounds / chemistry
  • Spectroscopy, Fourier Transform Infrared
  • Thionucleotides / chemistry*
  • ras Proteins / chemistry

Substances

  • Nitroso Compounds
  • Thionucleotides
  • P(3)-1-(2-nitro)phenylethylguanosine 5'-O-triphosphate
  • Guanosine Triphosphate
  • ras Proteins