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Conduction in protein and methylglyoxal‐protein complexes
Author(s) -
Lewis T. J.
Publication year - 2009
Publication title -
international journal of quantum chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.484
H-Index - 105
eISSN - 1097-461X
pISSN - 0020-7608
DOI - 10.1002/qua.560140717
Subject(s) - methylglyoxal , chemistry , chemical physics , valence (chemistry) , thermal conduction , conductivity , acceptor , conduction band , electron transport chain , electron , condensed matter physics , physics , biochemistry , thermodynamics , quantum mechanics , organic chemistry , enzyme
Recent measurements by Pethig and others, reported in this symposium, of the electrical conductivity of proteins and protein‐methylglyoxal complexes are remarkably similar to those reported for many other noncrystalline solids outside the biological sphere. The concepts of hoppingor activated charge carrier motion frequently adopted to explain the behavior of the latter are adopted to explain the behavior of the proteins. These concepts involve an electronic band model in which charge transfers are considered to occur between localized states via “hole” transport in a valence band derived from the polypeptide backbone of the proteins. It is suggested that when methylglyoxal complexes with protein, additional and specific electron‐acceptor states are introduced with a consequent increase in hole density in the protein valence bands and enhanced low‐frequency and steady‐state conduction.