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Selective Removal of the Type 2 Cu from Blue Oxidases. Properties and Functional Role of the Copper Centres
Author(s) -
Morpurgo Laura,
Graziani Maria Teresa,
Avigliano Luciana,
Desideri Alessandro,
Mondovi Bruno
Publication year - 1981
Publication title -
israel journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.908
H-Index - 54
eISSN - 1869-5868
pISSN - 0021-2148
DOI - 10.1002/ijch.198100007
Subject(s) - chemistry , copper , redox , acceptor , laccase , enzyme , electron acceptor , electron transfer , copper protein , inorganic chemistry , photochemistry , combinatorial chemistry , biochemistry , organic chemistry , physics , condensed matter physics
A brief review is given of the available methods for removing the Type 2 Cu from blue oxidases and of the properties of the modified enzymes. The Type 2 Cu appears to be essential to the catalytic activity of the enzymes and to participate, at least in tree laccase, both in the reductive and oxidative processes. The Type 2 Cu is also involved in water exchange with bulk solution and in the binding of anions and of H 2 O 2 . It is connected with the other copper types, as its removal considerably affects their redox potential and the intensity of the 330 nm charge transfer band associated with a two‐electron acceptor.
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