Editorial: Microbial Biominerals: Toward New Functions and Resource Recovery

Staicu, Lucian C.; Hullebusch, Eric D. van; Ackerson, Christopher J.

doi:10.3389/fmicb.2021.796374

Cited by 6 publications

(4 citation statements)

References 7 publications

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“…This species may show promise for bioremediation of selenium contamination-an area where previous work has been done collecting biogenically produced Se(0) from wastewater. 37,38 Transmission electron microscopy (TEM) and electron tomography of the P. moraviensis stanleyae shows B50 nm diameter intracellular SeNPs. There is no apparent membrane or protein structure surrounding these SeNPs.…”

Section: Cloneable Contrastmentioning

confidence: 99%

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Cloneable inorganic nanoparticles

Hendricks,

Guilliams,

Cohen

et al. 2023

Chem. Commun.

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Section: Cloneable Contrastmentioning

confidence: 99%

“…This species may show promise for bioremediation of selenium contamination—an area where previous work has been done collecting biogenically produced Se(0) from wastewater. 37,38…”

Section: Introductionmentioning

confidence: 99%

Cloneable inorganic nanoparticles

Hendricks,

Guilliams,

Cohen

et al. 2023

Chem. Commun.

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“…It is expected that modification of metal(loid) reductase enzyme substrate specificities will benefit several academic and industrial applications. Biomining and bioremediation of metals are nascent fields that currently rely on intact microbes to extract metals from heterogeneous mixtures. − Molecular mechanisms underlying the microbial extractions are scarcely characterized. , Identification, improvement, or alteration of enzymatic processes underlying biomining may facilitate the use of “greener” approaches to metal(loid) mining.…”

Section: Introductionmentioning

confidence: 99%

Laboratory Evolution of Metalloid Reductase Substrate Recognition and Nanoparticle Product Size

Hendricks,

Cohen,

McEwen

et al. 2024

ACS Chem. Biol.

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Glutathione reductase-like metalloid reductase (GRLMR) is an enzyme that reduces selenodiglutathione (GS-Se-SG), forming zerovalent Se nanoparticles (SeNPs). Error-prone polymerase chain reaction was used to create a library of ∼10,000 GRLMR variants. The library was expressed in BL21Escherichia coli in liquid culture with 50 mM of SeO 3 2− present, under the hypothesis that the enzyme variants with improved GS-Se-SG reduction kinetics would emerge. The selection resulted in a GRLMR variant with two mutations. One of the mutations (D−E) lacks an obvious functional role, whereas the other mutation is L− H within 5 Å of the enzyme active site. This mutation places a second H residue within 5 Å of an active site dicysteine. This GRLMR variant was characterized for NADPH-dependent reduction of GS-Se-SG, GSSG, SeO 3 2− , SeO 4 2− , GS-Te-SG, and TeO 3 2− . The evolved enzyme demonstrated enhanced reduction of SeO 3 2− and gained the ability to reduce SeO 4 2−. This variant is named selenium reductase (SeR) because of its emergent broad activity for a wide variety of Se substrates, whereas the parent enzyme was specific for GS-Se-SG. This study overall suggests that new biosynthetic routes are possible for inorganic nanomaterials using laboratory-directed evolution methods.

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“…It is expected that modification of metal(loid) reductase enzyme substrate specificities will benefit several academic and industrial applications. Biomining and bioremediation of metals are nascent fields which currently rely on intact microbes to extract metals from heterogeneous mixtures [36][37][38][39][40] . Molecular mechanisms underlying the microbial extractions are scarcely characterized 41,42 .…”

Section: Introductionmentioning

confidence: 99%

Laboratory Evolution of Metalloid Reductase Substrate Specificity and Product Size

Hendricks,

Cohen,

McEwen

et al. 2023

Preprint

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: Glutathione Reductase-Like Metalloid Reductase (GRLMR) is an enzyme that reduces selenodiglutathione (GS-Se-SG), forming zerovalent Se nanoparticles (SeNPs). Error prone polymerase chain reaction was used to create a library of ~10,000 GRLMR variants. The library was expressed in BL21 Escherichia coli in liquid culture with 50 mM of SeO32- present, under the hypothesis that the enzyme variants with improved GS-Se-SG reduction kinetics would emerge. The selection resulted in a GRLMR variant with 2 mutations. One of the mutations (D to E) lacks an obvious functional role, whereas the other mutation is L to H within 5 Å of the enzyme active site. This mutation places a second H residue within 5Å of an active site dicysteine. This GRLMR variant was characterized for NADPH dependent reduction of GS-Se-SG, GSSG, SeO32-, SeO42-, GS-Te-SG and TeO32-. The evolved enzyme demonstrated enhanced reduction of SeO32- and gained ability to reduce SeO42-. This variant is named Selenium Reductase (SeR) because of its emergent broad activity for a wide variety of Se substrates, whereas the parent enzyme was specific for GS-Se-SG. This study overall suggests that new biosynthetic routes are possible for inorganic nanomaterials using laboratory directed evolution methods.

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Editorial: Microbial Biominerals: Toward New Functions and Resource Recovery

Cited by 6 publications

References 7 publications

Cloneable inorganic nanoparticles

Cloneable inorganic nanoparticles

Laboratory Evolution of Metalloid Reductase Substrate Recognition and Nanoparticle Product Size

Laboratory Evolution of Metalloid Reductase Substrate Specificity and Product Size

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