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