Abstract:
:Singlet oxygen reacts preferentially with three amino acids in proteins, His, Trp and Met. In order to study the specific molecular events that result from such oxidations, calf alpha-crystallin was photooxidized in the presence of uroporphyrin and the reactions were investigated by high performance liquid chromatography peptide mapping using a photodiode array detector followed by fast atom bombardment mass spectrometry (FAB-MS). From these studies, the following conclusions can be inferred: (1) Upon photooxidation residue Met-68 of the B chain is oxidized to Met sulfoxide, whereas residue Trp-60 remains intact. (2) Two of the 16 His residues in alpha-crystallin are photooxidized with an apparent pKa of ca 7.0 (3) FAB-MS analysis suggests that residue Lys-166 close to the C-terminal end of the A chain forms a cross-link with the His-7 residue close to the N-terminal end of the A chain. This may be either an inter- or intramolecular cross-link.
journal_name
Photochem Photobioljournal_title
Photochemistry and photobiologyauthors
Dillon J,Chiesa R,Wang RH,McDermott Mdoi
10.1111/j.1751-1097.1993.tb02330.xsubject
Has Abstractpub_date
1993-03-01 00:00:00pages
526-30issue
3eissn
0031-8655issn
1751-1097journal_volume
57pub_type
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