Properties of microsolvated ions: from the microenvironment of chromophore and alkali metal ions in proteins to negative ions in water clusters.
Here we discuss the fascinating chemistry and physics of microsolvated ions that bridge the transition from bare ions in gas phase to ions in solution. Such ions occur in many situations in biochemistry and are crucial for several functions; metal ions, for example, must remove their water shell to pass through ion pumps in membranes. Furthermore, only a few water molecules are buried in the hydrophobic pockets of proteins where they are bound to charged amino acid residues or ionic chromophores. Another aspect is the reactivity of microsolvated ions and the importance in atmospheric, organic and inorganic chemistry. We close by a discussion of the stability of molecular dianions, and how hydration affects the electronic binding energy. There is a vast literature on microsolvated ions, and in this review we are far from being comprehensive, rather we mainly bring examples of our own work.
Nielsen
Steen Brøndsted
SB
Department of Physics and Astronomy, University of Aarhus, Ny Munkegade, DK-8000 Aarhus C, Denmark. sbn@phys.au.dk
Andersen
Lars H
LH
D000838:Anions / Q000737:chemistry*; D049452:Green Fluorescent Proteins / Q000737:chemistry; D008672:Metals, Alkali / Q000737:chemistry*; D000432:Methanol / Q000737:chemistry; D015221:Potassium Channels / Q000737:chemistry; D011506:Proteins / Q000737:chemistry*; D012996:Solutions / Q000737:chemistry; D013499:Surface Properties; D014867:Water / Q000737:chemistry*
D000838:Anions; D008672:Metals, Alkali; D015221:Potassium Channels; D011506:Proteins; D012996:Solutions; D014867:Water; D049452:Green Fluorescent Proteins; D000432:Methanol