Development, Synthesis and Characterization of Biomimetic ...
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Characterization of Ligands SalenH 2 and BPG were characterized by 1 H NMR. 1 H NMR is used elucidate the structure of compound by measuring the number and chemical shift of protons. SalenH 2 : BPG: Characterization of Metal Complexes UV-Visible Spectra of Copper Complexes UV-Visible and IR Spectra of Manganese Complex Metalloenzymes are proteins that catalyze a specific reaction and contain metals that are tightly bound at the active site. Hemoglobin is a common metalloprotein that transfers O 2 in the blood. A subclass of metalloenzymes are dioxygenases. Dioxygenases transfer both oxygen atoms of O 2 into substrate. They have the ability to cleave and degrade aromatic compounds and play an important role in many biological functions, such as mammalian metabolism. 1 A specific dioxygenase, Quercetin 2,3 Dioxygenase (QDO), is unique in that it is the only known dioxygenase that is copper dependent. The copper center is bound to 3 histidines, 1 glutamate, and the antioxidant quercetin. 2 QDO is found in bacteria, where they use the enzyme to degrade aromatic compounds. Aromatic compounds are one of the most prevalent and persistent pollutants in the environment. A synthetic model that mimics the active site of QDO, could be used for possible bioremediation purposes. Characterization Future Work • Synthesize and characterize Fe 2+ (BPG) complex to model the active site of quercetin dioxygenase. • Study reactivity of Fe 2+ (BPG) and substrates. Acknowledgements University of Wisconsin – Eau Claire Chemistry Department University of Wisconsin – Eau Claire Material Science Program Student Blugold Commitment Differential Tuition funds through the UW- Eau Claire Faculty/Student Research Collaboration Grants program Synthesis Synthesis of Ligands SalenH 2 4 : N,N-bis(2-pyridlymethyl)glycine)(BPG) 3 : 1. Que, Lawrence; Ho, R. Y. N. Dioxygen Activation by Enzymes with Mononuclear Non-Heme Iron Active Sites. Chem. Rev. 1996, 96, 2607–2624. 2. Fusetti, F.; Schröter, K. H.; Steiner, R. A.; van Noort, P. I.; Pijning, T.; Rozeboom, H. J.; Kalk, K. H.; Egmond, M. R.; Dijkstra, B. W. Crystal Structure of the Copper-Containing Quercetin 2,3-Dioxygenase from Aspergillus Japonicus. Struct. Lond. Engl. 1993 2002, 10, 259–268. Steiner, R. A.; Kalk, K. H.; Dijkstra, B. W. Anaerobic Enzyme⋅substrate Structures Provide Insight into the Reaction Mechanism of the Copper-Dependent Quercetin 2,3-Dioxygenase. Proc. Natl. Acad. Sci. 2002, 99, 16625–16630. 3. Cox, D.; Benkovic, J.; Bloom, L.M.; Bradley, F.C.; Nelson, M.J.; Que, L.; Wallick. J.M. Chem. Soc. 1998, 110, 2027 4. Shaabani S.; Darbari R. Elixir Org. Chem. 2013, 55, 12764-12766 Introduction Development, Synthesis and Characterization of Biomimetic Model Complexes Elizabeth Brandes, Kristin Sahr and Ariel Schuelke and Dr. Roslyn M. Theisen Department of Chemistry, University of Wisconsin - Eau Claire Research Goals • Synthesize ligands that mimic the 3-His-1-Carboxylate coordination • Synthesize and characterize metal complexes • Study reactivity of metal complexes and substrates 0 0.2 0.4 0.6 0.8 1 1.2 200 300 400 500 600 700 800 Absorbance (AU) Wavelength (nm) [Cu(II)(Salen)] (green) in MeOH N N O O Cu II 0 0.2 0.4 0.6 0.8 1 1.2 1.4 200 300 400 500 600 700 800 Absorbance Wavelength(nm) Cu(BPG) (blue) and Cu(BPG)(Quercetin)(green) in MeOH Cu(BPG) Cu(BPG)(Quercetin) O O OH OH HO OH OH Quercetin 2,3 dioxygenase O 2 CO O CO 2 H O OH HO OH OH N N N O O Cu II 2PF 6 - References 0 0.2 0.4 0.6 0.8 1 1.2 200 300 400 500 600 700 800 Absorbance (AU) Wavelength (nm) UV/Vis Spectrum of Mn(Salen) in MeOH 0.00 10.00 20.00 30.00 40.00 50.00 60.00 70.00 80.00 90.00 100.00 1,200 1,400 1,600 1,800 2,000 2,200 2,400 % Transmittance Frequency (cm -1 ) FT-IR Spectrum of Mn(Salen) in mineral oil N N O O M 2+ M 2+ salt NaOH, MeOH M 2+ salt NaOH, MeOH AgPF 6 or NaBPh 4 N N N O O M ν(C=N) = 1540cm -1 λ = 394nm λ =351nm λ =255 and 287nm λ =265 and 302nm
Transcript of Development, Synthesis and Characterization of Biomimetic ...
Characterization of LigandsSalenH2 and BPG were characterized by
1H NMR. 1H NMR is used elucidate the
structure of compound by measuring the number and chemical shift of protons.
SalenH2: BPG:
Characterization of Metal Complexes
UV-Visible Spectra of Copper Complexes
UV-Visible and IR Spectra of Manganese Complex
Metalloenzymes are proteins that catalyze a specific reaction and contain metals that are tightly bound at the active site. Hemoglobin is a common
metalloprotein that transfers O2 in the blood.
A subclass of metalloenzymes are dioxygenases. Dioxygenases transfer both oxygen atoms of O2 into substrate. They have the ability to cleave and
degrade aromatic compounds and play an important role in many
biological functions, such as mammalian metabolism.1
A specific dioxygenase, Quercetin 2,3 Dioxygenase (QDO), is unique in that
it is the only known dioxygenase that is copper dependent. The copper
center is bound to 3 histidines, 1 glutamate, and the antioxidant quercetin.2
QDO is found in bacteria, where they use the enzyme to degrade aromatic
compounds. Aromatic compounds are one of the most prevalent and
persistent pollutants in the environment. A synthetic model that mimics the active site of QDO, could be used for possible bioremediation purposes.
Characterization
Future Work• Synthesize and characterize Fe2+(BPG) complex to model the active site of quercetin dioxygenase.
• Study reactivity of Fe2+(BPG) and substrates.
AcknowledgementsUniversity of Wisconsin – Eau Claire Chemistry DepartmentUniversity of Wisconsin – Eau Claire Material Science Program
Student Blugold Commitment Differential Tuition funds through the
UW- Eau Claire Faculty/Student Research Collaboration Grants program
SynthesisSynthesis of LigandsSalenH2
4:
N,N-bis(2-pyridlymethyl)glycine)(BPG)3:
1. Que, Lawrence; Ho, R. Y. N. Dioxygen Activation by Enzymes with Mononuclear Non-Heme Iron Active
Sites. Chem. Rev. 1996, 96, 2607–2624. 2. Fusetti, F.; Schröter, K. H.; Steiner, R. A.; van Noort, P. I.; Pijning, T.; Rozeboom, H. J.; Kalk, K. H.; Egmond, M. R.; Dijkstra, B. W. Crystal Structure of the Copper-Containing Quercetin 2,3-Dioxygenase from Aspergillus
Japonicus. Struct. Lond. Engl. 1993 2002, 10, 259–268. Steiner, R. A.; Kalk, K. H.; Dijkstra, B. W. Anaerobic Enzyme⋅substrate Structures Provide Insight into the Reaction Mechanism of the Copper-Dependent
Quercetin 2,3-Dioxygenase. Proc. Natl. Acad. Sci. 2002, 99, 16625–16630. 3. Cox, D.; Benkovic, J.; Bloom, L.M.; Bradley, F.C.; Nelson, M.J.; Que, L.; Wallick. J.M. Chem. Soc. 1998, 110,
20274. Shaabani S.; Darbari R. Elixir Org. Chem. 2013, 55, 12764-12766
Introduction
Development, Synthesis and Characterization of Biomimetic Model Complexes Elizabeth Brandes, Kristin Sahr and Ariel Schuelke and Dr. Roslyn M. Theisen
Department of Chemistry, University of Wisconsin - Eau Claire
Research Goals• Synthesize ligands that mimic the 3-His-1-Carboxylate coordination• Synthesize and characterize metal complexes
• Study reactivity of metal complexes and substrates
0
0.2
0.4
0.6
0.8
1
1.2
200 300 400 500 600 700 800
Ab
sorb
an
ce (A
U)
Wavelength (nm)
[Cu(II)(Salen)] (green) in MeOH
N N
O O
CuII
0
0.2
0.4
0.6
0.8
1
1.2
1.4
200 300 400 500 600 700 800
Ab
so
rban
ce
Wavelength(nm)
Cu(BPG) (blue) and Cu(BPG)(Quercetin)(green) in MeOH
Cu(BPG)
Cu(BPG)(Quercetin)
O
O
OH
OH
HO
OH
OHQuercetin
2,3 dioxygenase
O2 COO
CO2H
O
OH
HO
OH
OH
N
N
N
O
O
CuII
2PF6-
References
0
0.2
0.4
0.6
0.8
1
1.2
200 300 400 500 600 700 800
Ab
so
rban
ce (A
U)
Wavelength (nm)
UV/Vis Spectrum of Mn(Salen) in MeOH
0.00
10.00
20.00
30.00
40.00
50.00
60.00
70.00
80.00
90.00
100.00
1,2001,4001,6001,8002,0002,2002,400
% T
ran
sm
itta
nce
Frequency (cm-1)
FT-IR Spectrum of Mn(Salen) in mineral oil
N N
O O
M2+M2+ salt
NaOH, MeOH
M2+ salt
NaOH, MeOH
AgPF6 or NaBPh4
N
N
N
O
O
M
ν(C=N) = 1540cm-1
λ = 394nm
λ =351nmλ =255 and 287nm
λ =265 and 302nm
