Solvent isotope effects on the structure and function of mitochondrial membranes in aqueous media.
Solvent isotope effects on the structure and function of mitochondrial membranes in aqueous media.
复制标题
溶剂同位素对水介质中线粒体膜的结构和功能的影响。
DOI:
10.1016/0003-9861(74)90505-0
复制
发表时间:
1974
影响因子:
3.9
通讯作者:
Y. Hatefi
中科院分区:
文献类型:
--
作者:
W. Hanstein;K. A. Davis;Y. Hatefi
The structural stability of mitochondrial membranes and the enzyme complexes of the electron transport system, and the solubility of a small molecular-weight nonelectrolyte (2-methylnaphthoquinone), have been studied as a function of water structure. D 2 O, which is considered to be more structured than ordinary water, and H 2 O were used as solvents in conjunction with chaotropic ions which have been shown to break down water structure. Assays for membrane stability were (a) resolution with respect to solubilization of at least one constituent enzyme, and (b) chaotrope-induced lipid autoxidation, which is a measure of structural destabilization. Solvent isotope effects expressed as the quotient of chaotrope (NaClO 4) concentration (C D C H) necessary to elicit the same effect were found to be (a) essentially constant for each system over a wide range of NaClO 4 concentration, and (b) limited to the narrow range of 1.2–1.8 in all tests despite significant differences in the systems studied and the measurements used. The magnitude and the constancy of the isotope effects indicate that increased membrane stability (ie, the increased strength of hydrophobic interactions in membranes), and decreased water-solubility of nonelectrolytes in D 2 O are mainly due to the higher degree of order of the deuterated solvent. Thus, in the mitochondrial electron transport chain and many other enzyme systems where solvent isotope effects have been observed, the isotope effect appears to be more a consequence of conformational changes imposed on the enzymes by D 2 O, because it is a more structured solvent, rather than an indication of direct involvement of protons or the water molecule in the reaction mechanisms.