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Non‐thermal effects of microwaves on proteins: thermophilic enzymes as model system
Author(s) -
Porcelli Marina,
Cacciapuoti Giovanna,
Fusco Stefania,
Massa Rita,
d'Ambrosio Guglielmo,
Bertoldo Costanzo,
De Rosa Mario,
Zappia Vincenzo
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(96)01505-0
Subject(s) - sulfolobus solfataricus , thermophile , circular dichroism , enzyme , chemistry , hydrolase , microwave , biochemistry , glycogen phosphorylase , biophysics , biology , physics , quantum mechanics , archaea , gene
Two thermophilic and thermostable enzymes, isolated from Sulfolobus solfataricus , S ‐adenosylhomocysteine hydrolase and 5′‐methylthioadenosine phosphorylase, were exposed to 10.4 GHz microwave radiation in order to discriminate between thermal and non‐thermal microwave effects. The exposure causes a non‐thermal, irreversible and time‐dependent inactivation of both enzymes; the inactivation rate is related to the energy absorbed and is independent of the enzyme concentration. The influence of salts on enzyme inactivation has also been investigated. Conformational changes of S ‐adenosylhomocysteine hydrolase, detected by fluorescence and circular dichroism techniques, suggest that microwaves induce protein structural rearrangements not related to temperature.