The dynamics of H-bonds of the hydration shells of ions, ATPase and NE-activated adenylyl cyclase on the coupling of energy and signal transduction

TL;DR

This paper investigates the hydration shells of ions and their roles in energy and signal transduction, revealing how hydration dynamics influence enzyme activity, ion transport, and memory processes.

Contribution

It provides new insights into hydration shell dynamics of ions and their impact on ATPase activity, signal transduction, and memory mechanisms, using glycerol titration and other biochemical analyses.

Findings

Hydration shells are involved in ATPase transition states.

Ion hydration influences enzyme activity and signal transduction.

Mg2+ plays a key role in activating adenylyl cyclase and memory processes.

Abstract

Glycerol titration distinguished from free water the local hydration shell involved in ATPase transition from active to inactive, with cooperativity for water n=16. Rat brain cortex: NE-stimulated and its basal AC in the absence of free Mg2+, allows a refractive state of AC with negative cooperativity for MgATP and ATP4-. The erythrocyte-Hb system operates as a metabolic sensor to match glucose availability with the release of Hb-carried, O2 and Mg2+ at CSF. [Mg(H2O)6](H2O)122+ by chelating either a protein or ATP4- losses most of its hydration shell. The ion pump ATPase by forming ADP3- releases an incompletely hydrated Mg2+, which could capture H2O from either [Na.(H2O)6]+ or [K.(H2O)6]+. Thus, sieve-sizing their hydration shells for fitting into Na+-pump channels. An AC refractory period may participate in STM. Mg2+ with cooperativity n=3.7 activates NE-AC. CREB-generated receptors coupled by Mg2+ may modulate hydration shells-dependent oscillations for retrieval of LTM