Response of the regulatory oscillatory behavior of copperII-containing ECTO-NOX proteins and of CuIICl2 in solution to electromagnetic fields.
A family of cell surface and growth-related proteins, designated ECTO-NOX proteins, carry out both copper-dependent NADH and hydroquinone oxidation and protein disulfide-thiol interchange. The two activities they catalyze alternate to generate a regular period of 24min in length for the constitutive CNOX. Unexpectedly, Cu(II) salts alone in solution catalyze NADH (or hydroquinone) oxidation with a similar oscillatory pattern. Both patterns consist of five maxima, two of which at physiological temperatures are separated by an interval of 6min and three of which are separated by intervals of 4.5min [6min+4 (4.5min)]. EXAFS and infrared spectroscopic measurements on pure water have shown previously that the ratios of ortho and para isomers of the hydrogen atoms of water occur on a similar time scale and produce regular patterns of unequally spaced oscillations similar to those observed with ECTO-NOX proteins and Cu(II)Cl(2) solutions. Here, we provide results from Cu(II)Cl(2) solutions that demonstrate that ECTO-NOX-/Cu(II)-catalyzed oscillations in NADH oxidation are phased by exposure to low frequency electromagnetic fields.
Morré
D James
DJ
Department of Medicinal Chemistry and Molecular Pharmacology, Hansen Life Sciences Research Building, Purdue University, 201 S. University Street, West Lafayette, IN 47907-2064, United States. morre@pharmacy.purdue.edu
Jiang
Ziying
Z
Marjanovic
Milorad
M
Orczyk
John
J
Morré
Dorothy M
DM
D002462:Cell Membrane / Q000378:metabolism; D003300:Copper / Q000737:chemistry*; D004574:Electromagnetic Fields; D018546:Hypocotyl / Q000378:metabolism; D009247:NADH, NADPH Oxidoreductases / Q000737:chemistry* / Q000378:metabolism; D010084:Oxidation-Reduction; D013025:Glycine max / Q000378:metabolism
D003300:Copper; D009247:NADH, NADPH Oxidoreductases