Dye-sensitized selective photo-oxidation of cysteine.

@article{Jori1969DyesensitizedSP,
  title={Dye-sensitized selective photo-oxidation of cysteine.},
  author={Giulio Jori and Guido Galiazzo and Ernesto Scoffone},
  journal={International journal of protein research},
  year={1969},
  volume={1 4},
  pages={
          289-98
        }
}
The phtalein derivative cresol red and the fuchsin dye crystal violet have been found to sensitize the selective photo-oxidation of cysteine, both free and incorporated into a protein. The specificity for cysteine of these dyes was checked in aqueous solution over the pH range 2.5-9, as well as in aqueous acetic acid. In acidic solutions, cysteine is quantitatively converted to cysteic acid; on the contrary, in neutral or alkaline media, the photo-oxidative process is competed by a dark… 
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Probing the topography of proteins in solution by photosensitized oxidation. The catalytic region of papain.
FURTHER STUDIES ON THE CRYSTAL‐VIOLET‐SENSITIZED PHOTOOXIDATION OF CYSTEINE TO CYSTEIC ACID
Abstract—Crystal violet sensitizes the selective photooxidation of cysteine to cysteic acid; hydrogen peroxide is also formed as an end product. The participation of singlet oxygen in the…
The sensitized fading of triphenylmethane dyes in polymer films. Part 2
THE DYE-SENSITIZED PHOTOOXIDATION OF BIOLOGICAL MACROMOLECULES*
TLDR
The first formal description of the sensitized photooxidation of biological macromolecules was made by Professor von Tappeiner and his students in Munich in 1903 and since that time, photo-dynamic studies have been made on a large number of different proteins, mainly crystalline enzymes, as well as on polysaccharides and nucleic acids.
PROFLAVINE‐SENSITIZED SELECTIVE PHOTOOXXDATION OF THE TRYPTOPHYL RESIDUES IN PAPAIN
TLDR
It is demonstrated that the protein can exist in several more or less denatured conformations depending on the surrounding medium, and the solution conformation of some areas of the papain molecule may be different from that in the crystal state as deduced from X‐ray diffraction studies.
DYE‐SENSITIZED PHOTOOXIDATION OF PROTEINS *
TLDR
The present paper is concerned with the protein aspects of photodynamic effects on proteins, and not all cases of the dye-sensitized photooxidation of proteins can be interpreted in terms of a singlet-oxygen mechanism.
Paramagnetic metal ions as protectors of selected regions of protein molecules from photodynamic action.
Probing the topography of proteins in solution by photosensitized oxidation. Irradiation of nitrophenyl derivatives of ribonuclease A.
TLDR
It appears that this method yields quite reliable and refined information about the tertiary structure of proteins, provided that the introduced sensitizer is inserted in fixed positions within the protein matrix.
Photosensitized oxidation of elastase. Selective modification of the tryptophyl residues.
PHOTOOXIDATION OF LANTHANIDE ION‐LYSOZYME COMPLEXES. A NEW APPROACH TO THE EVALUATION OF INTRAMOLECULAR DISTANCES IN PROTEINS
TLDR
On the basis of the atomic coordinates of lysozyme in the crystal state, it is possible to define a “quenching radius” for the various lanthanide ions; these radii could in turn be used to evaluate intramolecular distances in proteins of unknown tertiary structure, by identifying the amino acid residues that are protected or photooxidized upon irradiation of complexes between the given protein and several different lanthanides.
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