Mono-hydrated hydroxide ions

Deactivation (weak) from the adjoining ring does not prevent facile disubstitution of 4-methyl- and 4-phenyl-2,7-dichloro-1,8-naphthyridines wdth alkoxides (65°, 30 min), p-phenetidine (ca. 200°, 2 hr), hydrazine hydrate (100°, 8 hr), or diethylaminoethylmer-captide (in xylene, 145°, 24 hr) mono-substitution has not been reported. Nor does stronger deactivation prevent easy 2-oxonation of 5,7-dimethoxy-l-methylnaphthyridinium iodide wdth alkaline ferricyanide via hydroxide ion attack adjacent to the positive charge and loss of hydride ion by oxidation. 

Metal-mediated reactions involving water are essential to life and catalytic industrial processes [1-3]. In biological systems, metalloenzymes containing various divalent metal ions catalyze the hydrolysis of amide, carboxylic ester and phosphate ester bonds using both mono- and multinuclear active-site structural motifs [4—6], Mononuclear metal centers are also found within the active sites of enzymes that catalyze the hydration, or the addition of water, to CO2 [Zn(II)] and nitriles [Co(III)/Fe(III)j [7-10]. In many of these processes, formation of a metal hydroxide moiety via deprotonation of a metal-coordinated water molecule is a key proposed step in the reaction pathway. Thus, a substantial amount of research over the past several years has been directed at dehneating how the structural and electronic environments of biological metal ions influence the pKa of a metal-bound water molecule. In this regard, studies directed at the preparation, characterization and elucidation of the reactivity of discrete metal aqua and hydroxo complexes have been paramoimt [11-13]. 

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