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LASER FLASH PHOTOLYSIS AND INACTIVATION OF CARBOXYPEPTIDASE A *
Author(s) -
Lee Joon Y.,
Grossweiner L. I.
Publication year - 1978
Publication title -
photochemistry and photobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 131
eISSN - 1751-1097
pISSN - 0031-8655
DOI - 10.1111/j.1751-1097.1978.tb07657.x
Subject(s) - flash photolysis , chemistry , adduct , photochemistry , photodissociation , radiolysis , zinc , molecule , radical , organic chemistry , kinetics , physics , quantum mechanics , reaction rate constant
— Laser photolysis of CPA at 265 nm photoionizes 3 to 4 Trp residues per molecule inactivated, leading to e ‐ aq and the disulfide bridge electron adduct. The electron adduct is formed by an internal process and is not involved in the activity loss. Based on this work and published photochemical and pulse radiolysis studies on CPA it is proposed that photolysis of a key Trp residue, possibly Trp 73 adjacent to zinc ligand Glu 72 , mediates release of the zinc ion and consequent loss of peptidase activity.