journal article·2020-05

Biomanufacturing of nanocrystals using protein biocatalysts

Tatiana V. Avramenko, Yuri N Shkryl, Galina N Veremeichik, Victor P Bulgakov

Journal of Nanoparticle Research· Volume 22· Issue 5
Publisher page

Abstract

Being in the intermediate state between bulk material and single particle, nanocrystals possess extraordinary properties combining the best of both. Synthesis of such advanced materials is currently of big demand. Two basic approaches are applied for the fabrication of nanoscaled materials, including chemical synthesis and bio-inspired engineering. The strategy of bio-inspired synthesis is a promising alternative to harsh methods since it does not require extreme synthesis conditions, is environmentally friendly, and allows the combination of materials of various origins, designing nanocomposites with new properties. Based on the idea of natural inspiration, proteins involved in the process of biomineralization, performed in living organisms, have been investigated. The remarkable catalytic properties of these proteins determine their use as a platform for the bioinspired synthesis of nanocrystalline materials. Here, we review the fundamentals of biomineralization, experimental strategies, and recent engineering developments focusing on the synthesis of semiconductor, magnetic, and metal(loid) oxide nanocrystals within a biomimetic approach.
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Research context

OpenAlex topics: Enzyme Production and Characterization · Diatoms and Algae Research · Metal Extraction and Bioleaching

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References (100+)

Show source-provided references
1. Aguilar-Camacho JM, Doonan L, McCormack GP (2019) Evolution of the main skeleton-forming genes in sponges (phylum Porifera) with special focus on the marine Haplosclerida (class Demospongiae). Mol Phylogenet Evol 131:245–253. https://doi.org/10.1016/j.ympev.2018.11.01510.1016/j.ympev.2018.11.015 ↗
2. Aguilar-Camacho JM, McCormack GP (2019) Silicatein expression in Haliclona indistincta (phylum Porifera, order Haplosclerida) at different developmental stages. Dev Genes Evol 229:35–41. https://doi.org/10.1007/s00427-019-00627-710.1007/s00427-019-00627-7 ↗
3. Alivisatos P (2004) The use of nanocrystals in biological detection. Nat Biotechnol 22:47–52. https://doi.org/10.1038/nbt92710.1038/nbt927 ↗
4. Amemiya Y, Arakaki A, Staniland SS, Tanaka T, Matsunaga T (2007) Controlled formation of magnetite crystal by partial oxidation of ferrous hydroxide in the presence of recombinant magnetotactic bacterial protein Mms6. Biomaterials 28:5381–5389. https://doi.org/10.1016/j.biomaterials.2007.07.05110.1016/j.biomaterials.2007.07.051 ↗
5. André R, Tahir MN, Schröder HCC, Müller WEG, Tremel W (2011) Enzymatic synthesis and surface deposition of tin dioxide using silicatein-alpha. Chem Mater 23:5358–5365. https://doi.org/10.1021/cm201977c10.1021/cm201977c ↗
6. Arakaki A, Webb J, Matsunaga T (2003) A novel protein tightly bound to bacterial magnetic particles in Magnetospirillum magneticum strain AMB-1. J Biol Chem 278:8745–8750. https://doi.org/10.1074/jbc.M21172920010.1074/jbc.M211729200 ↗
7. Arakaki A, Masuda F, Amemiya Y, Tanaka T, Matsunaga T (2010) Control of the morphology and size of magnetite particles with peptides mimicking the Mms6 protein from magnetotactic bacteria. J Colloid Interface Sci 343:65–70. https://doi.org/10.1016/j.jcis.2009.11.04310.1016/j.jcis.2009.11.043 ↗
8. Arakaki A, Yamagishi A, Fukuyo A, Tanaka M, Matsunaga T (2014) Co-ordinated functions of Mms proteins define the surface structure of cubo-octahedral magnetite crystals in magnetotactic bacteria. Mol Microbiol 93:554–567. https://doi.org/10.1111/mmi.1268310.1111/mmi.12683 ↗
9. Arakaki A, Kikuchi D, Tanaka M, Yamagishi A, Yoda T, Matsunaga T (2016) Comparative subcellular localization analysis of magnetosome proteins reveals a unique localization behavior of Mms6 protein onto magnetite crystals. J Bacteriol 198:2794–2802. https://doi.org/10.1128/JB.00280-1610.1128/JB.00280-16 ↗
10. Baesman SM, Bullen TD, Dewald J, Zhang D, Curran S, Islam FS, Beveridge TJ, Oremland RS (2007) Formation of tellurium nanocrystals during anaerobic growth of bacteria that use Te oxyanions as respiratory electron acceptors. J Appl Environ Microbiol 73:2135–2143. https://doi.org/10.1128/AEM.02558-0610.1128/AEM.02558-06 ↗
11. Bai HJ, Zhang ZM, Guo Y, Yang GE (2009) Biosynthesis of cadmium sulfide nanoparticles by photosynthetic bacteria Rhodopseudomonas palustris. Colloids Surf B: Biointerfaces 70:142–146. https://doi.org/10.1016/j.colsurfb.2008.12.02510.1016/j.colsurfb.2008.12.025 ↗
12. Bai L, Ouyang Y, Song J, Xu Z, Liu W, Hu J, Wang Y, Yuan F (2019) Synthesis of metallic nanocrystals: from noble metals to base metals. Materials (Basel) 12:1497. https://doi.org/10.3390/ma1209149710.3390/ma12091497 ↗
13. Barber-Zucker S, Keren-Khadmy N, Zarivach R (2016) From invagination to navigation: the story of magnetosome-associated proteins in magnetotactic bacteria. Protein Sci 25:338–351. https://doi.org/10.1002/pro.282710.1002/pro.2827 ↗
14. Barber-Zucker S, Zarivach R (2017) A look into the biochemistry of magnetosome biosynthesis in magnetotactic bacteria. ACS Chem Biol 12:13–22. https://doi.org/10.1021/acschembio.6b0100010.1021/acschembio.6b01000 ↗
15. Bazylinski DA, Frankel RB, Heywood BR, Mann S, King JW, Donaghay PL, Hanson AK (1995) Controlled biomineralization of magnetite (Fe3O4) and greigite (Fe3S4) in a magnetotactic bacterium. Appl Environ Microbiol 61:3232–323910.1128/AEM.61.9.3232-3239.1995 ↗
16. Blakemore RB (1975) Magnetotactic bacteria. Science 190:377–379. https://doi.org/10.1126/science.17067910.1126/science.170679 ↗
17. Boles MA, Ling D, Hyeon T, Talapin DV (2016) The surface science of nanocrystals. Nat Mater 15:141–153. https://doi.org/10.1038/nmat452610.1038/nmat4526 ↗
18. Brutchey RL, Yoo ES, Morse DE (2006) Biocatalytic synthesis of a nanostructured and crystalline bimetallic perovskite-like barium oxofluorotitanate at low temperature. J Am Chem Soc 128:10288–10294. https://doi.org/10.1021/ja063107g10.1021/ja063107g ↗
19. Chang T-L, Zhan H, Liang D, Liang JF (2015) Nanocrystal technology for drug formulation and delivery. Front Chem Sci Eng 9:1–14. https://doi.org/10.1007/s11705-015-1509-310.1007/s11705-015-1509-3 ↗
20. Curran CD, Lu L, Jia Y, Kiely CJ, Berger BW, McIntosh S (2017) Direct single-enzyme biomineralization of catalytically active ceria and ceria-zirconia nanocrystals. ACS Nano 11:3337–3346. https://doi.org/10.1021/acsnano.7b0069610.1021/acsnano.7b00696 ↗
21. Currie HA, Perry CC (2007) Silica in plants: biological, biochemical and chemical studies. Ann Bot 100:1383–1389. https://doi.org/10.1093/aob/mcm24710.1093/aob/mcm247 ↗
22. De Windt W, Aelterman P, Verstraete W (2005) Bioreductive deposition of palladium (0) nanoparticles on Shewanella oneidensis with catalytic activity towards reductive dechlorination of polychlorinated biphenyls. Environ Microbiol 7:314–325. https://doi.org/10.1111/j.1462-2920.2005.00696.x10.1111/j.1462-2920.2005.00696.x ↗
23. Dunleavy R, Lu L, Kiely CJ, McIntosh S, Berger BW (2016) Single-enzyme biomineralization of cadmium sulfide nanocrystals with controlled optical properties. Proc Natl Acad Sci U S A 113:5275–5280. https://doi.org/10.1073/pnas.152363311310.1073/pnas.1523633113 ↗
24. Dworak L, Matylitsky VV, Breus VV, Braun M, Basché Е, Wachtveitl J (2011) Ultrafast charge separation at the CdSe/CdS core/shell quantum dot/methylviologen interface: implications for nanocrystal solar cells. J Phys Chem C 115:3949–3955. https://doi.org/10.1021/jp111574w10.1021/jp111574w ↗
25. Erickson SD, Smith TJ, Moses LM, Watt RK, Colton JS (2015) Non-native Co-, Mn-, and Ti-oxyhydroxide nanocrystals in ferritin for high efficiency solar energy conversion. Nanotechnology 26:015703. https://doi.org/10.1088/0957-4484/26/1/01570310.1088/0957-4484/26/1/015703 ↗
26. Figuerola A, van Huis M, Zanella M, Genovese A, Marras S, Falqui A, Zandbergen HW, Cingolani R, Manna L (2010) Epitaxial CdSe-Au nanocrystal heterostructures by thermal annealing. Nano Lett 10:3028–3036. https://doi.org/10.1021/nl101482q10.1021/nl101482q ↗
27. Fortin D, Southam G, Beveridge T (1994) Nickel sulfide, iron-nickel sulfide and iron sulfide precipitation by a newly isolated Desulfotomaculum species and its relation to nickel resistance. FEMS Microbiol Ecol 14:121–132. https://doi.org/10.1111/j.1574-6941.1994.tb00099.x10.1111/j.1574-6941.1994.tb00099.x ↗
28. Gadd GM, Griffiths A (1978) Microorganisms and heavy metal toxicity. Microb Ecol 4:303–317. https://doi.org/10.1007/BF0201327410.1007/BF02013274 ↗
29. García-Rodríguez R, Hendricks MP, Cossairt BM, Liu H, Owen JS (2013) Conversion reactions of cadmium chalcogenide nanocrystal precursors. Chem Mater 25:1233–1249. https://doi.org/10.1021/cm303564210.1021/cm3035642 ↗
30. Huang W (2016) Oxide nanocrystal model catalysts. Acc Chem Res 49:520–527. https://doi.org/10.1021/acs.accounts.5b0053710.1021/acs.accounts.5b00537 ↗
31. Jarvis M, Krishnan V, Mitragotri S (2018) Nanocrystals: a perspective on translational research and clinical studies. Bioeng Transl Med 4:5–16. https://doi.org/10.1002/btm2.1012210.1002/btm2.10122 ↗
32. Jayaseelan C, Rahuman AA, Kirthi AV, Marimuthu S, Santhoshkumar T, Bagavan A, Gaurav K, Karthik L, Rao KV (2012) Novel microbial route to synthesize ZnO nanoparticles using Aeromonas hydrophila and their activity against pathogenic bacteria and fungi. Spectrochim Acta A Mol Biomol Spectrosc 90:78–84. https://doi.org/10.1016/j.saa.2012.01.00610.1016/j.saa.2012.01.006 ↗
33. Kagan (2019) Flexible colloidal nanocrystal electronics. Chem Soc Rev 48:1626–1641. https://doi.org/10.1039/C8CS00629F10.1039/C8CS00629F ↗
34. Kisailus D, Choi JH, Weaver JC, Yang W, Morse DE (2005) Enzymatic synthesis and nanostructural control of gallium oxide at low temperature. Adv Mater 17:314–318. https://doi.org/10.1002/adma.20040081510.1002/adma.200400815 ↗
35. Klaus T, Joerger R, Olsson E, Granqvist CG (1999) Silver-based crystalline nanoparticles, microbially fabricated. Proc Natl Acad Sci U S A 96:13611–13614. https://doi.org/10.1073/pnas.96.24.1361110.1073/pnas.96.24.13611 ↗
36. Kolinko I, Lohße A, Borg S, Raschdorf O, Jogler C, Tu Q, Pósfai M, Tompa E, Plitzko JM, Brachmann A, Wanner G, Müller R, Zhang Y, Schüler D (2014) Biosynthesis of magnetic nanostructures in a foreign organism by transfer of bacterial magnetosome gene clusters. Nat Nanotechnol 9:193–197. https://doi.org/10.1038/nnano.2014.1310.1038/nnano.2014.13 ↗
37. Konishi Y, Tsukiyama T, Tachimi T, Saitoh N, Nomura T, Nagamine S (2007) Microbial deposition of gold nanoparticles by the metal-reducing bacterium Shewanella algae. Electrochim Acta 53:186–192. https://doi.org/10.1016/j.electacta.2007.02.07310.1016/j.electacta.2007.02.073 ↗
38. Kovalenko MV, Manna L, Cabot A, Hens Z, Talapin DV, Kagan CR, Klimov VI, Rogach AL, Reiss P, Milliron DJ, Guyot-Sionnnest P, Konstantatos G, Parak WJ, Hyeon T, Korgel BA, Murray CB, Heiss W (2015) Prospects of nanoscience with nanocrystals. ACS Nano 9:1012–1057. https://doi.org/10.1021/nn506223h10.1021/nn506223h ↗
39. Kowalik IA, Szwacki NG, Niño MÁ, Luqued FJ, Arvanitis D (2019) Stable antiferromagnetic nanocrystals for room temperature applications: the case of iron nitride. J Mater Chem C 7:9474–9480. https://doi.org/10.1039/C9TC02334H10.1039/C9TC02334H ↗
40. Kröger N, Deutzmann R, Sumper M (1999) Polycationic peptides from diatom biosilica that direct silica nanosphere formation. Science 286:1129–1132. https://doi.org/10.1126/science.286.5442.112910.1126/science.286.5442.1129 ↗
41. Kröger N, Lorenz S, Brunner E, Sumper M (2002) Self-assembly of highly phosphorylated silaffins and their function in biosilica morphogenesis. Science 29:584–586. https://doi.org/10.1126/science.107622110.1126/science.1076221 ↗
42. Kumar K, Liu Q, Hiller J, Schedel C, Maier A, Meixner A, Braun K, Lauth J, Scheele M (2019) Fast, infrared-active optical transistors based on dye-sensitized CdSe nanocrystals. ACS Appl Mater Interfaces 11:48271–48280. https://doi.org/10.1021/acsami.9b1823610.1021/acsami.9b18236 ↗
43. Lefèvre CT, Menguy N, Abreu F, Lins U, Pósfai M, Prozorov T, Pignol D, Frankel RB, Bazylinski DA (2011) A cultured greigite-producing magnetotactic bacterium in a novel group of sulfate-reducing bacteria. Science 334:1720–1723. https://doi.org/10.1126/science.121259610.1126/science.1212596 ↗
44. Lengke MF, Fleet ME, Southam G (2006) Synthesis of platinum nanoparticles by reaction of filamentous cyanobacteria with platinum(IV)-chloride complex. Langmuir. 22:7318–7323. https://doi.org/10.1021/la060873s10.1021/la060873s ↗
45. Li L, Curran C, Christopher K, Berger B, Mcintosh S (2016) Morphology and composition of biomineralized ceria and ceria-zirconia nanocrystals. Microsc Microanal 22:250–251. https://doi.org/10.1017/S143192761600210510.1017/S1431927616002105 ↗
46. Li H, Jia С, Meng X, Li H (2018) Chemical synthesis and applications of colloidal metal phosphide nanocrystals. Front Chem 6:652. https://doi.org/10.3389/fchem.2018.0065210.3389/fchem.2018.00652 ↗
47. Liu CY, Holman ZC, Kortshagen UR (2009) Hybrid solar cells from P3HT and silicon nanocrystals. Nano Lett 9:449–452. https://doi.org/10.1021/nl803433810.1021/nl8034338 ↗
48. Lohße A, Ullrich S, Katzmann E, Borg S, Wanner G, Richter M, Voigt B, Schweder T, Schüler D (2011) Functional analysis of the magnetosome island in Magnetospirillum gryphiswaldense: the mamAB operon is sufficient for magnetite biomineralization. PLoS One 6:e25561. https://doi.org/10.1371/journal.pone.002556110.1371/journal.pone.0025561 ↗
49. Lohße A, Borg S, Raschdorf O, Kolinko I, Tompa E, Pósfai M, Faivre D, Baumgartner J, Schülera D (2014) Genetic dissection of the mamAB and mms6 operons reveals a gene set essential for magnetosome biogenesis in Magnetospirillum gryphiswaldense. J Bacteriol 196:2658–2669. https://doi.org/10.1128/JB.01716-1410.1128/JB.01716-14 ↗
50. Lohße A, Kolinko I, Raschdorf O, Uebe R, Borg S, Brachmann A, Plitzko JM, Müller R, Zhang Y, Schüler D (2016) Overproduction of magnetosomes by genomic amplification of biosynthesis-related gene clusters in a magnetotactic bacterium. Appl Environ Microbiol 82:3032–3041. https://doi.org/10.1128/AEM.03860-1510.1128/AEM.03860-15 ↗
51. Lopez-Moreno R, Fernández-Vivas A, Valverde-Tercedor C, Azuaga Fortes AI, Casares Atienza S, Rodriguez-Navarro AB, Zarivach R, Jimenez-Lopez C (2017) Magnetite nanoparticles biomineralization in the presence of the magnetosome membrane protein MamC: effect of protein aggregation and protein structure on magnetite formation. Cryst Growth Des 17:1620–1629. https://doi.org/10.1021/acs.cgd.6b0164310.1021/acs.cgd.6b01643 ↗
52. Lu P, Lu M, Wang H, Sui N, Shi Z, Yu WW (2019) Metal halide perovskite nanocrystals and their applications in optoelectronic devices. 1:430–459. https://doi.org/10.1002/inf2.1203110.1002/inf2.12031 ↗
53. Ma K, Zhao H, Zheng X, Sun H, Hu L, Zhu L, Shen Y, Luo T, Dai H, Wang J (2017) NMR studies of the interactions between AMB-1 Mms6 protein and magnetosome Fe3O4 nanoparticles. J Mater Chem 5:2888–2895. https://doi.org/10.1039/C7TB00570A10.1039/C7TB00570A ↗
54. Maleke M, Valverde A, Vermeulen JG, Cason E, Gomez-Arias A, Moloantoa K, Coetsee-Hugo L, Swart H, van Heerden E, Castillo J (2019) Biomineralization and bioaccumulation of europium by a thermophilic metal-resistant bacterium. Front Microbiol 10:81. https://doi.org/10.3389/fmicb.2019.0008110.3389/fmicb.2019.00081 ↗
55. McVey BFP, König D, Cheng X, O'Mara PB, Seal P, Tan X, Tahini HA, Smith SC, Gooding JJ, Tilley RD (2018) Synthesis, optical properties and theoretical modelling of discrete emitting states in doped silicon nanocrystals for bioimaging. Nanoscale 10:15600–15607. https://doi.org/10.1039/C8NR05071F10.1039/C8NR05071F ↗
56. Mi JL, Jensen TN, Christensen M, Tyrsted C, Jørgensen JE, Iversen BB (2011) High-temperature and high-pressure aqueous solution formation, growth, crystal structure, and magnetic properties of BiFeO3 nanocrystals. Chem Mater 23:1158–1165. https://doi.org/10.1021/cm102575w10.1021/cm102575w ↗
57. Moodelly D, Kowalik P, Bujak P, Pron A, Reiss P (2019) Synthesis, photophysical properties and surface chemistry of chalcopyrite-type semiconductor nanocrystals. J Mater Chem C 7:11665–11709. https://doi.org/10.1039/C9TC03875B10.1039/C9TC03875B ↗
58. Müller WE, Boreiko A, Schlossmacher U et al (2008a) Identification of a silicatein(−related) protease in the giant spicules of the deep-sea hexactinellid Monorhaphis chuni. J Exp Biol 211(Pt 3):300–309. https://doi.org/10.1242/jeb.00819310.1242/jeb.008193 ↗
59. Müller WE, Link T, Schröder HC, Korzhev M, Neufurth M, Brandta D, Wang X (2014) Dissection of the structure-forming activity from the structure-guiding activity of silicatein: a biomimetic molecular approach to print optical fibers. J Mater Chem B 2:5368–5377. https://doi.org/10.1039/C4TB00801D10.1039/C4TB00801D ↗
60. Müller WE, Schlossmacher U, Eckert C, Krasko A, Boreiko A, Ushijima H, Wolf SE (2007) Analysis of the axial filament in spicules of the demosponge Geodia cydonium: different silicatein composition in microscleres (asters) and megascleres (oxeas and triaenes). Eur J Cell Biol 86:473–487. https://doi.org/10.1016/j.ejcb.2007.06.00210.1016/j.ejcb.2007.06.002 ↗
61. Müller WE, Wang X, Kropf K et al (2008b) Silicatein expression in the hexactinellid Crateromorpha meyeri: the lead marker gene restricted to siliceous sponges. Cell Tissue Res 333:339–351. https://doi.org/10.1007/s00441-008-0624-610.1007/s00441-008-0624-6 ↗
62. Nag A, Chung DS, Dolzhnikov DS, Dimitrijevic NM, Chattopadhyay S, Shibata T, Talapin DV (2012) Effect of metal ions on photoluminescence, charge transport, magnetic and catalytic properties of all-inorganic colloidal nanocrystals and nanocrystal solids. J Am Chem Soc 134:13604–13615. https://doi.org/10.1021/ja301285x10.1021/ja301285x ↗
63. Ondič L, Varga M, Pelant I, Valenta J, Kromka A, Elliman RG (2017) Silicon nanocrystal-based photonic crystal slabs with broadband and efficient directional light emission. Sci Rep 7:5763. https://doi.org/10.1038/s41598-017-05973-y10.1038/s41598-017-05973-y ↗
64. Oremland RS, Herbel MJ, Blum JS, Langley S, Beveridge TJ, Ajayan PM, Sutto T, Ellis AV, Curran S (2004) Structural and spectral features of selenium nanospheres produced by Se-respiring bacteria. J Appl Environ Microbiol 70:52–60. https://doi.org/10.1128/AEM.70.1.52-60.200410.1128/AEM.70.1.52-60.2004 ↗
65. Peck HD Jr (1961) Enzymatic basis for assimilatory and dissimilatory sulfate reduction. J Bacteriol 82:933–93910.1128/JB.82.6.933-939.1961 ↗
66. Povarova NV, Markina NM, Baranov MS, Barinov NA, Klinov DV, Kozhemyako VB, Lukyanov KA (2018) A water-soluble precursor for efficient silica polymerization by silicateins. Biochem Biophys Res Commun 495:2066–2070. https://doi.org/10.1016/j.bbrc.2017.12.07510.1016/j.bbrc.2017.12.075 ↗
67. Prasad K, Jha AK, Kulkarni AR (2007) Lactobacillus assisted synthesis of titanium nanoparticles. Nanoscale Res Lett 2:248–250. https://doi.org/10.1007/s11671-007-9060-x10.1007/s11671-007-9060-x ↗
68. Prozorov T, Palo P, Wang L, Nilsen-Hamilton M, Jones D, Orr D, Mallapragada SK, Narasimhan B, Canfield PC, Prozorov R (2007) Cobalt ferrite nanocrystals: out-performing magnetotactic bacteria. ACS Nano 1:228–233. https://doi.org/10.1021/nn700194h10.1021/nn700194h ↗
69. Rahn-Lee L, Byrne ME, Zhang M, Le Sage D, Glenn DR, Milbourne T, Walsworth RL, Vali H, Komeili A (2015) A genetic strategy for probing the functional diversity of magnetosome formation. PLoS Genet 11:e1004811. https://doi.org/10.1371/journal.pgen.100481110.1371/journal.pgen.1004811 ↗
70. Raschdorf O, Müller FD, Pósfai M, Plitzko JM, Schüler D (2013) The magnetosome proteins MamX, MamZ and MamH are involved in redox control of magnetite biomineralization in Magnetospirillum gryphiswaldense. Mol Microbiol 89:872–886. https://doi.org/10.1111/mmi.1231710.1111/mmi.12317 ↗
71. Rawlings AE, Bramble JP, Hounslow AM, Williamson MP, Monnington AE, Cooke DJ, Staniland SS (2016) Ferrous iron binding key to Mms6 magnetite biomineralisation: a mechanistic study to understand magnetite formation using pH titration and NMR spectroscopy. Chemistry 22:7885–7894. https://doi.org/10.1002/chem.20160032210.1002/chem.201600322 ↗
72. Rawlings AE, Bramble JP, Walker R, Bain J, Galloway JM, Staniland SS (2014) Self-assembled MmsF proteinosomes control magnetite nanoparticle formation in vitro. Proc Natl Acad Sci U S A 111:16094–16099. https://doi.org/10.1073/pnas.140925611110.1073/pnas.1409256111 ↗
73. Sadeghnejad A, Lu L, Kiely CJ, Berger BW, McIntosh S (2017) Single enzyme direct biomineralization of ZnS, ZnxCd1-xS and ZnxCd1-xS–ZnS quantum confined nanocrystals. RSC Adv 7:38490–38497. https://doi.org/10.1039/c7ra05586b10.1039/c7ra05586b ↗
74. Scheffel A, Gärdes A, Grünberg K, Wanner G, Schüler D (2008) The major magnetosome proteins MamGFDC are not essential for magnetite biomineralization in Magnetospirillum gryphiswaldense but regulate the size of magnetosome crystals. J Bacteriol 190:377–386. https://doi.org/10.1128/JB.01371-0710.1128/JB.01371-07 ↗
75. Schröder HC, Wiens M, Schloßmacher U, Brandt D, Müller WEG (2012) Silicatein-mediated polycondensation of orthosilicic acid: modeling of a catalytic mechanism involving ring formation. Silicon 4:33–38. https://doi.org/10.1007/s12633-010-9057-410.1007/s12633-010-9057-4 ↗
76. Shimizu K, Cha J, Stucky GD, Morse DE (1998) Silicatein alpha: cathepsin L-like protein in sponge biosilica. Proc Natl Acad Sci U S A 95:6234–6238. https://doi.org/10.1073/pnas.95.11.623410.1073/pnas.95.11.6234 ↗
77. Shkryl YN, Bulgakov VP, Veremeichik GN, Kovalchuk SN, Kozhemyako VB, Kamenev DG, Semiletova IV, Timofeeva YO, Shchipunov YA, Kulchin YN (2016) Bioinspired enzymatic synthesis of silica nanocrystals provided by recombinant silicatein from the marine sponge Latrunculia oparinae. Bioprocess Biosyst Eng 39:53–58. https://doi.org/10.1007/s00449-015-1488-210.1007/s00449-015-1488-2 ↗
78. Shkryl YN, Veremeichik GN, Kamenev DG, Gorpenchenko TY, Yugay YA, Mashtalyar DV, Nepomnyaschiy AV, Avramenko TV, Karabtsov AA, Ivanov VV, Bulgakov VP, Gnedenkov SV, Kulchin YN, Zhuravlev YN (2018a) Green synthesis of silver nanoparticles using transgenic Nicotiana tabacum callus culture expressing silicatein gene from marine sponge Latrunculia oparinae. Artif Cells Nanomed Biotechnol 46:1646–1658. https://doi.org/10.1080/21691401.2017.138824810.1080/21691401.2017.1388248 ↗
79. Shkryl YN, Veremeichik GN, Avramenko TV, Bulgakov VP, Semiletova IV, Shchipunov YA, Nepomnyaschiy AV, Voznesenskiy SS, Kovalchuk SN, Kozhemyako VB (2018b) Biomimetic synthesis of nanosized silica structures on a substrate with silicatein. Russ J Bioorg Chem 44:469–471. https://doi.org/10.1134/S013234231804018810.1134/S0132342318040188 ↗
80. Smith E, Nie S (2010) Semiconductor nanocrystals: structure, properties, and band gap engineering. Acc Chem Res 43:190–200. https://doi.org/10.1021/ar900106910.1021/ar9001069 ↗
81. Snee PT, Somers RC, Nair G, Zimmer JP, Bawendi MG, Nocera DG (2006) A ratiometric CdSe/ZnS nanocrystal pH sensor. J Am Chem Soc 128:13320–13321. https://doi.org/10.1021/ja061899910.1021/ja0618999 ↗
82. Spangler LC, Lu L, Kiely CJ, Berger BW, McIntosh SJ (2016) Biomineralization of PbS and PbS–CdS core–shell nanocrystals and their application in quantum dot sensitized solar cells. J Mater Chem A 4:6107–6115. https://doi.org/10.1039/C5TA10534J10.1039/C5TA10534J ↗
83. Spangler LC, Chu R, Lu L, Kiely CJ, Berger BW, McIntosh SJ (2017) Enzymatic biomineralization of biocompatible CuInS2, (CuInZn)S2 and CuInS2/ZnS core/shell nanocrystals for bioimaging. Nanoscale 9:9340–9351. https://doi.org/10.1039/C7NR02852K10.1039/C7NR02852K ↗
84. Speirs MJ, Balazs DM, Fang HH, Lai LH, Protesescu L, Kovalenko MV, Loi MA (2015) Origin of the increased open circuit voltage in PbS–CdS core–shell quantum dot solar cells. J Mater Chem A 3:1450–1457. https://doi.org/10.1039/C4TA04785K10.1039/C4TA04785K ↗
85. Spring S, Schleifer KH (1995) Diversity of magnetotactic bacteria. Syst Appl Microbiol 18:147–153. https://doi.org/10.1016/S0723-2020(11)80386-310.1016/S0723-2020(11)80386-3 ↗
86. Sumerel JL, Yang W, Kisailus D, Weaver JC, Choi JH, Morse DE (2003) Biocatalytically templated synthesis of titanium dioxide. Chem Mater 15:4804–4809. https://doi.org/10.1021/cm030254u10.1021/cm030254u ↗
87. Sumper M (2002) A phase separation model for the nanopatterning of diatom biosilica. Science 295:2430–2433. https://doi.org/10.1126/science.107002610.1126/science.1070026 ↗
88. Sumper M, Lorenz S, Brunner E (2003) Biomimetic control of size in the polyamine-directed formation of silica nanospheres. Angew Chem Int Ed 42:5192–5195. https://doi.org/10.1002/anie.20035221210.1002/anie.200352212 ↗
89. Tabatabaei Dakhili SY, Caslin SA, Faponle AS, Quayle P, de Visser SP, Wong LS (2017) Recombinant silicateins as model biocatalysts in organosiloxane chemistry. Proc Natl Acad Sci U S A 114:E5285–E5291. https://doi.org/10.1073/pnas.161332011410.1073/pnas.1613320114 ↗
90. Tahir MN, Eberhardt M, Therese HA, Kolb U, Theato P, Müller WEG, Schröder HC, Tremel W (2006) From single molecules to nanoscopically structured functional materials: Au nanocrystal growth on TiO2 nanowires controlled by surface-bound silicatein. Angew Chem Int Ed Eng 45:4803–4809. https://doi.org/10.1002/anie.20050377010.1002/anie.200503770 ↗
91. Tanaka M, Mazuyama E, Arakaki A, Matsunaga T (2011) MMS6 protein regulates crystal morphology during nano-sized magnetite biomineralization in vivo. J Biol Chem 286:6386–6392. https://doi.org/10.1074/jbc.M110.18343410.1074/jbc.M110.183434 ↗
92. Taoka A, Eguchi Y, Mise S, Oestreicher Z, Uno F, Fukumori Y (2014) A magnetosome-associated cytochrome MamP is critical for magnetite crystal growth during the exponential growth phase. FEMS Microbiol Lett 358:21–29. https://doi.org/10.1111/1574-6968.1254110.1111/1574-6968.12541 ↗
93. Tolbert SH, Alivisatos AP (1995) The wurtzite to rock salt structural transformation in CdSe nanocrystals under high pressure. J Chem Phys 102:4642–4656. https://doi.org/10.1063/1.46951210.1063/1.469512 ↗
94. Tyschenko IE, Volodin VA, Cherkov AG (2016) Enhanced germanium precipitation and nanocrystal growth in the Ge+ ion-implanted SiO2 films during high-pressure annealing. Solid State Commun 247:53–57. https://doi.org/10.1016/j.ssc.2016.07.01210.1016/j.ssc.2016.07.012 ↗
95. Valverde-Tercedor C, Montalbán-López M, Perez-Gonzalez T, Sanchez-Quesada MS, Prozorov T, Pineda-Molina E, Fernandez-Vivas MA, Rodriguez-Navarro AB, Trubitsyn D, Bazylinski DA, Jimenez-Lopez C (2015) Size control of in vitro synthesized magnetite crystals by the MamC protein of Magnetococcus marinus strain MC-1. Appl Microbiol Biotechnol 99:5109–5121. https://doi.org/10.1007/s00253-014-6326-y10.1007/s00253-014-6326-y ↗
96. Veremeichik GN, Shkryl YN, Bulgakov VP, Shedko SV, Kozhemyako VB, Kovalchuk SN, Krasokhin VB, Zhuravlev YN, Kulchin YN (2011) Occurrence of a silicatein gene in glass sponges (Hexactinellida: Porifera). Mar Biotechnol 13:810–819. https://doi.org/10.1007/s10126-010-9343-610.1007/s10126-010-9343-6 ↗
97. Wang CL, Maratukulam PD, Lum AM, Clark DS, Keasling JD (2000) Metabolic engineering of an aerobic sulfate reduction pathway and its application to precipitation of cadmium on the cell surface. Appl Environ Microbiol 66:4497–4502. https://doi.org/10.1128/AEM.66.10.4497-4502.200010.1128/AEM.66.10.4497-4502.2000 ↗
98. Wang CL, Lum AM, Ozuna SC, Clark DS, Keasling JD (2001) Aerobic sulfide production and cadmium precipitation by Escherichia coli expressing the Treponema denticola cysteine desulfhydrase gene. Appl Environ Microbiol 56:425–430. https://doi.org/10.1007/s00253010066010.1007/s002530100660 ↗
99. Wang X, Schloßmacher U, Wiens M, Batel R, Schröder HC, Müller WE (2012) Silicateins, silicatein interactors and cellular interplay in sponge skeletogenesis: formation of glass fiber-like spicules. FEBS J 279:1721–1736. https://doi.org/10.1111/j.1742-4658.2012.08533.x10.1111/j.1742-4658.2012.08533.x ↗
100. Wang S, Wang X, Draenert FG, Albert O, Schröder HC, Mailänder V, Mitov G, Müller WE (2014) Bioactive and biodegradable silica biomaterial for bone regeneration. Bone 67:292–304. https://doi.org/10.1016/j.bone.2014.07.02510.1016/j.bone.2014.07.025 ↗