Crystallizing extracellular protein reveals paths for silver mineralization and recovery

Published: 5 June 2025| Version 1 | DOI: 10.17632/rxxfjjrdr2.1
Contributors:
Fiaz Ahmad,
,
,

Description

Heavy metal pollution calls for green recovery strategies. In response to metal stress, bacteria secret extracellular proteins (ECPs), but the specific role of individual ECP in silver (Ag2+) mineralization and recovery remains unexplored. Here, we investigated how a single ECP from silver-hypertolerant Enterobacter cloacae mediates Ag²⁺ mineralization. Proteomics (LC-MS/MS, MALDI-TOF) identified the 15.6 kDa protein as an inosine-monophosphate dehydrogenase (ImpD) homolog, whose secretion peaks in medium containing 15.9 mg L⁻¹ Ag²⁺. Partially purified ImpD crystallized at 20–30 °C. Time-resolved in-situ crystallography and X-ray diffraction captured monomers assembling into donut-shaped hexamers that weave into thread-like lattices; these ordered scaffolds template orientation-specific nucleation of Ag-rich crystals, enabling quantitative silver capture from solution. This previously unrecognized single-protein mediated biomineralization mechanism reveals ECPs as programmable bio-lixiviants, offering a low-energy, solvent-free route to selective metal recovery and expanding the toolkit for biometallurgy and environmental remediation.

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Institutions

  • Northwestern Polytechnical University School of Life Sciences

Categories

X-Ray Crystallography, X-Ray Diffraction

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