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The redox‐mediated control of enzyme function and cellular structure
Author(s) -
Gascoyne Peter
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.560280724
Subject(s) - glutathione , redox , chemistry , cytoplasm , dithiol , disulfide bond , enzyme , biophysics , function (biology) , glutathione disulfide , biochemistry , microbiology and biotechnology , inorganic chemistry , biology
A theoretical study is presented in which the feasibility of the redox control of enzymic function and cellular structure is demonstrated. It is shown that dithiol‐ and disulfide‐dependent enzymes may be expected to show a strong activity dependence on the oxidation state of the cytoplasmic glutathione in living cells. Cellular structure that is dependent on interprotein disulfide bonds also shows a strong dependence on the glutathione status. Such redox control is only feasible when the cytoplasmic glutathione is at least 99% reduced. A redox control mechanism would require that a cellular machinery exist in order to control the oxidation status of the cytoplasmic glutathione. The existence of such a control machinery is proposed.