Scribd
Upload
2 views1 page

Iron Complexes and Spectroscopy Quiz

The document contains a quiz for CH 521 on Interpretative Molecular Spectroscopy, featuring questions on Mössbauer spectroscopy, optical activity in coordination complexes, circular dichroism (CD) spectral changes, and electron paramagnetic resonance (EPR) spectra. Key topics include the relationship between oxidation states and isomer shifts, the significance of Doppler velocity in Mössbauer spectroscopy, and the effects of pH on protein secondary structures. Additionally, it addresses the hyperfine structure in EPR spectra of various metal complexes.

Uploaded by

quick127tear
Copyright
© All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
Available Formats
Download as PDF, TXT or read online on Scribd
2 views1 page

Iron Complexes and Spectroscopy Quiz

The document contains a quiz for CH 521 on Interpretative Molecular Spectroscopy, featuring questions on Mössbauer spectroscopy, optical activity in coordination complexes, circular dichroism (CD) spectral changes, and electron paramagnetic resonance (EPR) spectra. Key topics include the relationship between oxidation states and isomer shifts, the significance of Doppler velocity in Mössbauer spectroscopy, and the effects of pH on protein secondary structures. Additionally, it addresses the hyperfine structure in EPR spectra of various metal complexes.

Uploaded by

quick127tear
Copyright
© All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
Available Formats
Download as PDF, TXT or read online on Scribd

CH 521- Interpretative Molecular Spectroscopy (Quiz) 07-11-2025

1. Two iron complexes show Mössbauer isomer shifts of δ = 1.20 mm s⁻¹ and δ = 0.25
mm s⁻¹ relative to α-Fe. Which compound corresponds to high-spin Fe(II) and which
to low-spin Fe(III)? Justify your answer based on the relationship between oxidation
state, Fe–ligand bond length, and 4s electron density at the nucleus.

2. In Mössbauer spectroscopy of ⁵⁷Fe, a Doppler velocity of 1 mm s⁻¹ corresponds to an


energy shift of 4.8 × 10⁻⁸ eV, while the natural linewidth (Γ) is 4.6 × 10⁻⁹ eV.
What Doppler velocity range (in mm s⁻¹) must be scanned to cover one natural
linewidth? Why is such fine velocity control critical in recording a Mössbauer
spectrum?

3. The Mössbauer isomer shifts (δ) for two iron-containing biological samples are:
Deoxyhemoglobin (Fe²⁺) → δ = 1.05 mm s⁻¹ Methemoglobin (Fe³⁺) → δ = 0.25 mm
s⁻¹
Explain the origin of the difference in δ values. How does the oxidation state of iron
influence the 4s electron density at the nucleus and the Fe–N bond length in the
porphyrin ring?

4. Explain why molecules such as [Co(en)₃]³⁺ exhibit optical activity, whereas


Co(NH₃)₆]³⁺ does not, in terms of the relationship between μE and μM. What symmetry
property of the molecule determines whether R = 0 or R ≠ 0?
5. Sketch and label the expected positive and negative Cotton effects, and explain how
the sign of the Cotton effect can be used to assign the absolute configuration of a chiral
metal complex, such as Δ-[Ru(bipy)₃]²⁺ versus Λ-[Ru(bipy)₃]²
6. Explain the change in CD spectral shape when poly-L-lysine goes from pH = 6 (α-
helix) to pH = 10.8 (β-sheet).
How would a metalloprotein, such as cytochrome c, show CD spectral changes upon
denaturation or oxidation of Fe³⁺ → Fe²⁺?

7. Why does [Mn(H₂O)₆]²⁺ exhibit six equally spaced hyperfine lines in its EPR spectrum?

8. What causes the weak half-field (Δmₛ = ±2) EPR transition observed in Ni(II)
complexes (S = 1)?

9. Why does K₃[Mo(CN)₈]⁵⁻ show six weak hyperfine lines from ⁹⁵Mo/⁹⁷Mo and a strong
central line from ⁹⁴Mo/⁹⁶Mo in its EPR spectrum?

10. Why does [Cu(H₂O)₆]²⁺ show g > 2.00 while [Ni(H₂O)₆]²⁺ shows g < 2.00 in EPR
spectra?

You might also like