67
Acknowledgment
This work was supported in part by the NSF ADVANCE (HRD1008643) fellowship to O.V.M.
References
1. Hakemian AS, Rosenzweig AC (2007) The
biochemistry of methane oxidation. Annu Rev
Biochem 76:223–241
2. Wallar BJ, Lipscomb JD (1996) Dioxygen activation by enzymes containing binuclear non- heme
iron clusters. Chem Rev 96(7):2625–2658
3. Merkx M, Kopp DA, Sazinsky MH, Blazyk JL,
Müller J, Lippard SJ (2001) Dioxygen activation and methane hydroxylation by soluble
methane monooxygenase: a tale of two irons
and three proteins. Angew Chem Int Ed Engl
40:2782–2807
4. Hoffman BM, Lukoyanov D, Yang Z-Y, Dean
DR, Seefeldt LC (2014) Mechanism of nitrogen fixation by nitrogenase: the next stage.
Chem Rev 114:4041–4062
5. Sakurai T, Kataoka K (2007) Basic and applied
features of multicopper oxidases, CueO, billirubin oxidase, and laccase. Chem Rec
7(4):220–229
6. Yu F, Cangelosi VM, Zastrow ML, Tegoni M,
Plegaria JS, Tebo AG, Mocny CS, Ruckthong
L, Qayyum H, Pecoraro VL (2014) Protein
design: toward functional metalloenzymes.
Chem Rev 114:3495–3578
7. Rufo CM, Moroz YS, Moroz OV, Stöhr J,
Smith TA, Hu X, DeGrado WF, Korendovych
IV (2014) Short peptides self-assemble to produce catalytic amyloids. Nat Chem 6:303–309
8. Friedmann MP, Torbeev V, Zelenay V, Sobol
A, Greenwald J, Riek R (2015) Towards prebiotic catalytic amyloids using high hroughput
screening. PLoS One 10:e0143948
9. Maeda Y, Makhlynets OV, Matsui H,
Korendovych IV (2016) Design of catalytic
peptides and proteins through rational and
combinatorial approaches. Annu Rev Biomed
Eng 18:311–328
10. Makhlynets OV, Gosavi PM, Korendovych IV
(2016) Short self-assembling peptides are able
to bind to copper and activate oxygen. Angew
Chem Int Ed Engl 55(31):9017–9020
11. Rasik CM, Brown MK (2014) Total synthesis
of gracilioether F: development and application
of Lewis acid promoted ketene-alkene [2+2]
cycloadditions and late-stage C-H oxidation.
Angew Chem Int Ed Engl 53:14522–14526
12. Punniyamurthy T, Rout L (2008) Recent
advances in copper-catalyzed oxidation of
organic compounds. Coord Chem Rev
252:134–154
13. Ikeda R, Sugihara J, Uyama H, Kobayashi S
(1996) Enzymatic oxidative polymerization
of 2,6-dimethylphenol. Macromolecules 29:
8702–8705
14. Baesjou PJ, Driessen WL, Challa G, Reedijk
J (1998) A kinetic study of the copper- catalyzed
oxidative coupling of 2,6-dimethylphenol. The
role of copper, base and phenol concentrations.
J Mol Catal A: Chem 135:273–283
15. Cassagnes L-E, Hervé V, Nepveu F, Hureau C,
Faller P, Collin F (2013) The catalytically active
copper-amyloid-beta state: coordination site
responsible for reactive species production.
Angew Chem Int Ed Engl 52:11110–11113
16. Solano F, Lucas-Elío P, López-Serrano D,
Fernández E, Sanchez-Amat A (2001)
Dimethoxyphenol oxidase activity of different
microbial blue multicopper proteins. FEMS
Microbiol Lett 204:175–181
17. Mattinen M-L, Maijala P, Nousiainen P, Smeds
A, Kontro J, Sipilä J, Tamminen T, Willför S,
Viikari L (2011) Oxidation of lignans and lignin model compounds by laccase in aqueous
solvent systems. J Mol Catal B: Enzym
72:122–129
18. Wan Y, Du Y, Miyakoshi T (2008) Enzymatic
catalysis of 2,6-dimethoxyphenol by laccases
and products characterization in organic solutions. Sci China Ser B: Chem 51(7):669–676
19. Reiss R, Ihssen J, Richter M, Eichhorn E,
Schilling B, Thöny-Meyer L (2013) Laccase
versus laccase-like multi-copper oxidase: a
comparative study of similar enzymes with
diverse substrate spectra. PLoS One 8(6):
e65633
20. Korendovych IV, Kim YH, Ryan AH, Lear JD,
DeGrado WF, Shandler SJ (2010) Computational
design of a self-assembling beta-peptide oligomer. Org Lett 12(22):5142–5145
21. Kataoka K, Komori H, Ueki Y, Konno Y,
Kamitaka Y, Kurose S, Tsujimura S, Higuchi Y,
Kano K, Seo D, Sakurai T (2007) Structure
and function of the engineered multicopper
Preparation and Screening of Amyloid Fibrils
Acknowledgment
This work was supported in part by the NSF ADVANCE (HRD1008643) fellowship to O.V.M.
References
1. Hakemian AS, Rosenzweig AC (2007) The
biochemistry of methane oxidation. Annu Rev
Biochem 76:223–241
2. Wallar BJ, Lipscomb JD (1996) Dioxygen activation by enzymes containing binuclear non- heme
iron clusters. Chem Rev 96(7):2625–2658
3. Merkx M, Kopp DA, Sazinsky MH, Blazyk JL,
Müller J, Lippard SJ (2001) Dioxygen activation and methane hydroxylation by soluble
methane monooxygenase: a tale of two irons
and three proteins. Angew Chem Int Ed Engl
40:2782–2807
4. Hoffman BM, Lukoyanov D, Yang Z-Y, Dean
DR, Seefeldt LC (2014) Mechanism of nitrogen fixation by nitrogenase: the next stage.
Chem Rev 114:4041–4062
5. Sakurai T, Kataoka K (2007) Basic and applied
features of multicopper oxidases, CueO, billirubin oxidase, and laccase. Chem Rec
7(4):220–229
6. Yu F, Cangelosi VM, Zastrow ML, Tegoni M,
Plegaria JS, Tebo AG, Mocny CS, Ruckthong
L, Qayyum H, Pecoraro VL (2014) Protein
design: toward functional metalloenzymes.
Chem Rev 114:3495–3578
7. Rufo CM, Moroz YS, Moroz OV, Stöhr J,
Smith TA, Hu X, DeGrado WF, Korendovych
IV (2014) Short peptides self-assemble to produce catalytic amyloids. Nat Chem 6:303–309
8. Friedmann MP, Torbeev V, Zelenay V, Sobol
A, Greenwald J, Riek R (2015) Towards prebiotic catalytic amyloids using high hroughput
screening. PLoS One 10:e0143948
9. Maeda Y, Makhlynets OV, Matsui H,
Korendovych IV (2016) Design of catalytic
peptides and proteins through rational and
combinatorial approaches. Annu Rev Biomed
Eng 18:311–328
10. Makhlynets OV, Gosavi PM, Korendovych IV
(2016) Short self-assembling peptides are able
to bind to copper and activate oxygen. Angew
Chem Int Ed Engl 55(31):9017–9020
11. Rasik CM, Brown MK (2014) Total synthesis
of gracilioether F: development and application
of Lewis acid promoted ketene-alkene [2+2]
cycloadditions and late-stage C-H oxidation.
Angew Chem Int Ed Engl 53:14522–14526
12. Punniyamurthy T, Rout L (2008) Recent
advances in copper-catalyzed oxidation of
organic compounds. Coord Chem Rev
252:134–154
13. Ikeda R, Sugihara J, Uyama H, Kobayashi S
(1996) Enzymatic oxidative polymerization
of 2,6-dimethylphenol. Macromolecules 29:
8702–8705
14. Baesjou PJ, Driessen WL, Challa G, Reedijk
J (1998) A kinetic study of the copper- catalyzed
oxidative coupling of 2,6-dimethylphenol. The
role of copper, base and phenol concentrations.
J Mol Catal A: Chem 135:273–283
15. Cassagnes L-E, Hervé V, Nepveu F, Hureau C,
Faller P, Collin F (2013) The catalytically active
copper-amyloid-beta state: coordination site
responsible for reactive species production.
Angew Chem Int Ed Engl 52:11110–11113
16. Solano F, Lucas-Elío P, López-Serrano D,
Fernández E, Sanchez-Amat A (2001)
Dimethoxyphenol oxidase activity of different
microbial blue multicopper proteins. FEMS
Microbiol Lett 204:175–181
17. Mattinen M-L, Maijala P, Nousiainen P, Smeds
A, Kontro J, Sipilä J, Tamminen T, Willför S,
Viikari L (2011) Oxidation of lignans and lignin model compounds by laccase in aqueous
solvent systems. J Mol Catal B: Enzym
72:122–129
18. Wan Y, Du Y, Miyakoshi T (2008) Enzymatic
catalysis of 2,6-dimethoxyphenol by laccases
and products characterization in organic solutions. Sci China Ser B: Chem 51(7):669–676
19. Reiss R, Ihssen J, Richter M, Eichhorn E,
Schilling B, Thöny-Meyer L (2013) Laccase
versus laccase-like multi-copper oxidase: a
comparative study of similar enzymes with
diverse substrate spectra. PLoS One 8(6):
e65633
20. Korendovych IV, Kim YH, Ryan AH, Lear JD,
DeGrado WF, Shandler SJ (2010) Computational
design of a self-assembling beta-peptide oligomer. Org Lett 12(22):5142–5145
21. Kataoka K, Komori H, Ueki Y, Konno Y,
Kamitaka Y, Kurose S, Tsujimura S, Higuchi Y,
Kano K, Seo D, Sakurai T (2007) Structure
and function of the engineered multicopper
Preparation and Screening of Amyloid Fibrils