Response of the regulatory oscillatory behavior of copperII-containing ECTO-NOX proteins and of CuIICl2 in solution to electromagnetic fields |
| |
Authors: | Morré D James Jiang Ziying Marjanovic Milorad Orczyk John Morré Dorothy M |
| |
Affiliation: | a 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 b Department of Foods and Nutrition, Purdue University, 700 W. State Street, West Lafayette, IN 47907, United States |
| |
Abstract: | 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 24 min in length for the constitutive CNOX. Unexpectedly, CuII 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 6 min and three of which are separated by intervals of 4.5 min [6 min + 4 (4.5 min)]. 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 CuIICl2 solutions. Here, we provide results from CuIICl2 solutions that demonstrate that ECTO-NOX-/CuII-catalyzed oscillations in NADH oxidation are phased by exposure to low frequency electromagnetic fields. |
| |
Keywords: | CopperII Hydroquinone (NADH) oxidase CNOX Molecular and biological time keeping Redox potential Low frequency electromagnetic fields Growth |
本文献已被 ScienceDirect PubMed 等数据库收录! |
|