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Austin, R. N.

Publications and source records attributed to Austin, R. N..

2 recordsLinked to original sources

Biophytometallurgy: biomining metals from plant resources

The physicochemical controls governing metal acquisition, release, and redistribution across biological interfaces remain poorly understood. Biophytometallurgy--the microbially assisted release and recovery of plant-associated metals--was used to probe the directionality of the mechanisms controlling nickel and rare earth element (REE) release from Phytolacca during solid-liquid extraction. Bulk characterization did not support a dominant crystalline REE-phosphate-like host in hydroponically enriched shoots. Dissolution and rebinding experiments instead revealed chemically accessible nickel and REE pools, the latter of which had behaviors consistent with apparent equilibrium-like partitioning under mildly acidic conditions. During sulfur biooxidation, Acidithiobacillus ferrooxidans promoted REE release while providing a competing cell-associated REE sink. Consequently, aqueous REE concentrations reflected net redistribution among the separable plant, solution, and microbial phases instead of dissolution alone. These results establish a framework for studying metal partitioning across complex and coupled biological systems and support a route for aqueous REE recovery from plants without thermochemical conversion to ash.

bioengineering↗

Metallothionein-3 attenuates the effect of Cu2+ ions on actin filaments

Metallothionein 3 (MT-3) is a cysteine-rich metal-binding protein that is expressed in the mammalian central nervous system and kidney. Various reports have posited a role for MT-3 in regulating the actin cytoskeleton by promoting the assembly of actin filaments. We generated purified, recombinant mouse MT-3 of known metal compositions, either with zinc (Zn), lead (Pb), or copper/zinc (Cu/Zn) bound. None of these forms of MT-3 accelerated actin filament polymerization in vitro, either with or without the actin binding protein profilin. Furthermore, using a co-sedimentation assay, we did not observe Zn-bound MT-3 in complex with actin filaments. Cu2+ ions on their own induced rapid actin polymerization, an effect that we attribute to filament fragmentation. This effect of Cu2+ is reversed by adding either EGTA or Zn-bound MT-3, indicating that either molecule can chelate Cu2+ from actin. Altogether, our data indicate that recombinant MT-3 does not directly bind actin but it does attenuate the Cu-induced fragmentation of actin filaments.

biochemistry↗