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Tutorial 3

The document discusses the effective magnetic moments of various nickel and iron complexes, analyzing their structures and bonding based on these values. It also explains the differences in spin state transitions between liquid and solid states in spin crossover systems and compares the O2-binding curves of hemoglobin and myoglobin, attributing the sigmoidal shape of hemoglobin to cooperative effects. The document emphasizes the role of subunit interactions in hemoglobin and the lack of cooperativity in myoglobin.

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2 views2 pages

Tutorial 3

The document discusses the effective magnetic moments of various nickel and iron complexes, analyzing their structures and bonding based on these values. It also explains the differences in spin state transitions between liquid and solid states in spin crossover systems and compares the O2-binding curves of hemoglobin and myoglobin, attributing the sigmoidal shape of hemoglobin to cooperative effects. The document emphasizes the role of subunit interactions in hemoglobin and the lack of cooperativity in myoglobin.

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spammehere24x7
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Tutorial 3 CH 105 2022

1. The following complexes have the indicated effective magnetic moments. Describe the
structure and bonding of the complexes on the basis of the µeff values (in B.M.).
(a) K2NiF6 (µeff = 0 B.M.)
(b) Ni(NH3)2Cl2 (µeff = 3.3 B.M.)
(c) Ni(PEt3)2Cl2 (µeff = 0.0 B.M.)
(d) Ni(Ph3AsO)2Cl2 (µeff = 3.95 B.M.)

2. For the following octahedral iron complex, the effective magnetic moment (magnetic
susceptibility) changes at 300 K (A, µeff = 6.18 BM, cMT = 4.8 cm3 K mol-1), 240 K (B, µeff
= 3.45 BM, cMT = 1.5 cm3 K mol-1) and 150 K (C, µeff = 0 BM, cMT = 0 cm3 K mol-1).
Write the electronic configuration of the iron ion in the complex at step A and step C?

3. For spin crossover systems, in the liquid state it is common to observe a gradual transition
from low spin to high spin as a function of temperature. In the solid state, however, there
is often an abrupt change in spin state at a certain temperature. Explain this difference and
rationalize.

4. Why is the O2-binding curve sigmoidal for hemoglobin; however, it is hyperbolic for
myoglobin?
Ans.

Cooperative effect in Hb. Interaction between different subunits via salt bridge interactions
to showcase the sigmoidal behavior.

Whereas in Mb, one single unit. No cooperativity effect. So hyperbolic behavior.

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