Site-Specific Conversion of Cysteine Thiols into Thiocyanate Creates an IR Probe for Electric Fields in Proteins
- 27 September 2006
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 128 (41) , 13356-13357
- https://doi.org/10.1021/ja0650403
Abstract
The nitrile stretching mode of the thiocyanate moiety is a nearly ideal probe for measuring the local electric field arising from the organized environment of the interior of a protein. Nitriles were introduced into three proteins: ribonuclease S (RNase S), human aldose reductase (hALR2), and the reaction center (RC) of Rhodobacter capsulatus, through a facile synthetic scheme for the transformation of cysteine residues into thiocyanatoalanine. Vibrational Stark effect spectroscopy and Fourier transform infrared spectroscopy on the modified proteins demonstrated that thiocyanate residues are a highly general tool for probing electrostatic fields in proteins.Keywords
This publication has 24 references indexed in Scilit:
- Vibrational Stark Effects Calibrate the Sensitivity of Vibrational Probes for Electric Fields in ProteinsBiochemistry, 2003
- Vibrational Stark Effects of Nitriles II. Physical Origins of Stark Effects from Experiment and Perturbation ModelsThe Journal of Physical Chemistry A, 2001
- Vibrational Stark Spectroscopy in Proteins: A Probe and Calibration for Electrostatic FieldsThe Journal of Physical Chemistry B, 1999
- STARK SPECTROSCOPY: Applications in Chemistry, Biology, and Materials ScienceAnnual Review of Physical Chemistry, 1997
- Motion of Spin-Labeled Side Chains in T4 Lysozyme. Correlation with Protein Structure and DynamicsBiochemistry, 1996
- Identification of the reactive cysteine residue in human placenta aldose reductaseBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1993
- Carbon-13 NMR of cyanylated flavodoxin from Megasphaera elsdenii and of thiocyanate model compoundsBiochemistry, 1992
- An Unlikely Sugar Substrate Site in the 1.65 Å Structure of the Human Aldose Reductase Holoenzyme Implicated in Diabetic ComplicationsScience, 1992
- Use of fluorine-19 nuclear magnetic resonance to study conformation changes in selectively modified ribonuclease SBiochemistry, 1971
- Selective cyanylation of sulfhydryl groupsJournal of the American Chemical Society, 1970