Soman-hydrolyzing and -detoxifying properties of an enzyme from a thermophilic bacterium.

An enzyme that hydrolyzes soman (1,2,2-trimethylpropyl methylphosphonofluoridate) and two other phosphonofluoridates, but does not hydrolyze DFP (diisopropylphosphorofluoridate), has been partially purified from a rod-shaped spore-forming gram-positive OT (obligate thermophilic) bacterium. The enzyme shows a marked Mn2+ stimulation, and in this and its substrate preference does not resemble the organophosphorus acid anhydrolase (sometimes termed DFPase) found in squid. Like the squid enzyme, it is not inhibited by mipafox (N,N'-diisopropylphosphordiamidofluoridate), is not inactivated by ammonium sulfate, and does hydrolyze the acetylcholinesterase-inhibitory pair of diastereoisomers of soman as well as the relatively noninhibitory pair, thus detoxifying soman. In these three properties the OT enzyme does not resemble the ubiquitous organophosphorus acid anhydrolase often purified from mammalian and bacterial sources by cold ethanol fractionation. Thus this phosphono-specific OT enzyme may have a natural substrate and a physiological role distinct from other organophosphorus acid anhydrolases.

Studies on the chelation of aluminum for neurobiological application.

The formation and strength of chelation of A1(III) with salicylic acid (SA), citric acid (CIT), ethylenediaminetetraacetic acid (EDTA), ethylenediamine-di-(o-hydroxyphenylacetic acid) (EDDHA), N,N'-di-(2-hydroxybenzyl)ethylenediamine-N,N'-diacetic acid (HBED), and some mixed ligand systems consisting of the above ligands were examined at an ionic strength of 0.12 M NaCl and 25.0 +/- 0.1 degrees C. All the ligands under consideration form strong chelates with A1(III). The order of the stabilities (log KML) of their A1(III) chelates are SA (13.7) less than EDTA (15.3) less than CIT (18.0) less than EDDHA (24.5) approximately equal to HBED (24.8). An equilibrium analysis of the A1(III)-SA (1:1), A1(III)-CIT (1:1) and A1(III)-SA-CIT (1:1:1) systems indicated the occurrence of hydrolysis and polymerization reactions in each one of them. The A1(III)-EDTA (1:1) chelate was found to undergo hydrolysis even at pH 5. However, EDDHA and HBED each formed a very stable mononuclear chelate with A1(III) and did not show hydrolytic or polymerization tendencies.