Evidence map›Paper›PMID 27118834›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

Single-enzyme biomineralization of cadmium sulfide nanocrystals with controlled optical properties.

Robert Dunleavy, Li Lu, Christopher J Kiely, Steven McIntosh, Bryan W Berger

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
6.2field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

35 citing papers in PubMed, 109 citations in OpenAlex.

  1. Article
  2. Cystathionine β-synthase TtCbs1 fromApplied and environmental microbiology · 2025
    Article
  3. Overexpression ofInternational journal of molecular sciences · 2025
    Article
  4. Article
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  7. Article
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  9. Article
  10. Article
  11. Cloneable inorganic nanoparticles.Chemical communications (Cambridge, England) · 2023
    Review
  12. Article
  13. Utilizing a divalent metal ion transporter to control biogenic nanoparticle synthesis.Journal of industrial microbiology & biotechnology · 2023
    Article
  14. A de novo protein catalyzes the synthesis of semiconductor quantum dots.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  15. Article
  16. Article
  17. Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Robert DunleavyDepartment of Chemical and Biomolecular Engineering, Lehigh University, Bethlehem, PA 18015;
Li LuDepartment of Materials Science and Engineering, Lehigh University, Bethlehem, PA 18015;
Christopher J KielyDepartment of Chemical and Biomolecular Engineering, Lehigh University, Bethlehem, PA 18015; Department of Materials Science and Engineering, Lehigh University, Bethlehem, PA 18015;
Steven McIntoshDepartment of Chemical and Biomolecular Engineering, Lehigh University, Bethlehem, PA 18015; bwb209@lehigh.edu stm310@lehigh.edu.
Bryan W BergerDepartment of Chemical and Biomolecular Engineering, Lehigh University, Bethlehem, PA 18015; Program in Bioengineering, Lehigh University, Bethlehem, PA 18015 bwb209@lehigh.edu stm310@lehigh.edu.
Lehigh University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nature has evolved several unique biomineralization strategies to direct the synthesis and growth of inorganic materials. These natural systems are complex, involving the interaction of multiple biomolecules to catalyze biomineralization and template growth. Herein we describe the first report to our knowledge of a single enzyme capable of both catalyzing mineralization in otherwise unreactive solution and of templating nanocrystal growth. A recombinant putative cystathionine γ-lyase (smCSE) mineralizes CdS from an aqueous cadmium acetate solution via reactive H2S generation from l-cysteine and controls nanocrystal growth within the quantum confined size range. The role of enzymatic nanocrystal templating is demonstrated by substituting reactive Na2S as the sulfur source. Whereas bulk CdS is formed in the absence of the enzyme or other capping agents, nanocrystal formation is observed when smCSE is present to control the growth. This dual-function, single-enzyme, aerobic, and aqueous route to functional material synthesis demonstrates the powerful potential of engineered functional material biomineralization.

Indexed as

Biological ProductsCadmium CompoundsCatalysisCrystallizationCystathionine gamma-LyaseEnzyme ActivationLightMaterials TestingMineralsMolecular ConformationNanoparticlesParticle SizeRefractometryScattering, RadiationSulfidesSurface PropertiesBiological ProductsCadmium Compoundscadmium sulfideCystathionine gamma-LyaseMineralsSulfidesbiomineralizationcadmium sulfideenzymenanoparticlequantum dot

Identifiers

PMID27118834
PMCPMC4868489
OpenAlexW2344008049

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.