Electronic Spectra

[Ti(H2O)6]3+
q Such transitions are referred to as d-d transitions
 The Beer-Lambert Law
q The Beer-Lambert Law (l specific):
A=ecl Sample
A = absorbance (unitless, A = log10 P0/P)
P0 P
e = molar absorptivity (L mol-1 cm-1)
l = path length of the sample (cm) (power in) (power out)
c = concentration (mol/L or M)
l in cm
Concentration Absorbance
Path length Absorbance
Molar Abs. Absorbance
 Information Contained in an Electronic Spectra
Spectral Features:
q Number of transitions.
q Energy of the transitions.
q Intensity of the transitions.
e
100 200 300 400 500
Wavelength (nm)
 Even Seemingly Simple Systems May Exhibit
More than One Transition
q The case of [Ti(H2O)6]3+, a d1 system
q Looking closely at the spectra, we
will see that there is a “shoulder”
in the peak.
q It indicates two transitions which
are close in energy.
q Since the energies of these
transitions are similar, the peaks
appear very close to each other.
 Energy of the Transitions: Δ is Relatable to Colour
q [Ti(H2O)6]3+ is a d1 complex. The single electron in the t2g orbitals absorb energy in
the form of light and gets promoted to the eg orbitals to show it’s purple color.
q For [Ti(H2O)6]3+, this corresponds to 493 nm (Δo = 20,300 cm-1 = 243 kJ/mol).
q For t2g1eg0 configuration:
stabilization energy = 243 x 0.4 = 97 kJ/mol,
this extra stabilization due to the splitting of d-orbitals called
crystal field stabilization energy (CFSE).
 Why are Intensities of Colours Different
[Fe(H2O)6]SO4 K4[Fe(CN)6]
q Intensity is related to the “probability” of a transition.
q The value of e is indicative of this probability.
q The probability is also referred to as a transition either being “allowed” or
“forbidden”.
q The Beer-Lambert Law (l specific):
A = absorbance (unitless, A = log10 P0/P)
e = molar absorptivity (L mol-1 cm-1)
A=ecl l = path length of the sample (cm)
c = concentration (mol/L or M)
 Laporte Rule
In a molecule or ion possessing center of symmetry, transitions are not allowed
between orbitals of same parity. Transitions are only possible between orbitals that
differ by Δl = ±1; ‘l’ is the orbital quantum number.
Examples of forbidden transitions are: s to s, d to d, p to f etc.
Tetrahedral geometry is not affected by this rule as it does not have a center of
symmetry.
As a consequence, ε for tetrahedral complexes are 100 times more than the ε for
octahedral complexes.
Even octahedral complexes lose their center of symmetry transiently due to
unsymmetrical vibrations. This leads to color in octahedral and square planar
complexes
 Symmetry (Laporte) Selection Rules
q Orbital parity is notated as “g” and “u” (for even and odd in German)
q Orbitals are of even parity (g) if the phase sign does not change on inversion
q Orbitals are of odd parity (u) if the phase sign changes on inversion
a not a a
center of center of
inversion inversion
a=b a≠b b
b
s-orbital p-orbital d-orbital
gerade (g) ungerade (u) gerade (g)
Hence, the Laporte selection rule implies that d-d transitions are
forbidden (while d-p, p-d are allowed)
 Symmetry (Laporte) Selection Rules
q A photon has 1 unit of angular momentum
q When a photon is absorbed or emitted, this momentum must be conserved
Dl = ±1 or:
‘s ↔ p’, ‘p ↔ d’, ‘d ↔ f’ etc allowed (Dl = ±1)
‘s ↔ d’, ‘p ↔ f’ etc forbidden (Dl = ±2)
‘s ↔ s’, ‘p ↔ p’ , ‘d ↔ d’, ‘f ↔ f’ etc forbidden (Dl = 0)
…so why do we see ‘d-d’ bands?
 ‘Relaxing’ The Orbital Selection Rule
q The selection rules are exact and cannot be circumnavigated
q It is our model which is too simple:
Ø the ligand-field transitions described so far are not between point
charges but between orbitals in molecules
Ø labelling the orbitals as ‘d’ (atomic orbitals) is incorrect if there is any
covalency
q For tetrahedral complexes, there can be mixing of d and p orbitals
through covalency
L L
L L
M M
L L
L L
A metal p-orbital overlaps A metal d-orbital overlaps
with ligand orbitals with the same ligand orbitals
 ‘Relaxing’ The Orbital Selection Rule
q This way of ‘relaxing’ the orbital selection rule is not available in octahedral
complexes
L L
in phase
L L L L
no overlap
L L L L
out of phase
L L
A metal p-orbital overlaps A metal d-orbital cannot overlap
with ligand orbitals with the same ligand orbitals
In general, no mixing of the ‘d’ and ‘p’ orbitals is possible if
the molecule has a centre of inversion (Laporte rule)
 Symmetry (Laporte) Selection Rules
q Then why are octahedral complexes coloured?
q Again our model is deficient:
Ø molecules are not rigid but are always vibrating
During this vibration, centre of
inversion is temporarily lost:
d-p mixing can occur
q Vibrational amplitude is small so deviation and mixing is small:
Ø octahedral complexes have lower intensity bands than tetrahedral
complexes
Ø the intensity of the bands increases with temperature as amplitude
increases
 Spin-forbidden and Spin-allowed Transitions
Any transition for which ΔS¹≠0 is strongly forbidden; that is, in order to be allowed, a
transition must involve no change in spin state.
Allowed Forbidden
[Mn(H2O)6]2+ has a d5 metal ion and is a high-spin complex. Electronic transitions are
not only Laporte-forbidden, but also spin-forbidden. The dilute solutions of Mn2+
complexes are therefore colorless.
Case in Point: Tetrahedral vs Octahedral Complexes
q As we have seen, a tetrahedron has no center of symmetry, and so orbitals in
such symmetry cannot be gerade. Hence the d-levels in a tetrahedral
complex are e and t2, with no ‘g’ for gerade.
q This largely overcomes the Laporte selection rules (enabled by d-p mixing), so
that tetrahedral complexes tend to be more intense in color than octahedral.
 Representative Values of e
Transition εmax (M-1cm-1)
Spin and Symmetry forbidden "d-d" bands 0.001 - 1
Spin allowed and Symmetry forbidden "d-d" bands 1 - 100
Spin and Symmetry allowed CT bands 103 - 5 x 104
q What are CT bands? CT refers to Charge Transfer transitions which are both
Laporte and Spin allowed and hence are very intense.
q Certain complexes such as MnO4-, CrO42- etc. are intensely coloured even
though they have metal ions without electrons in the d-orbitals. The colour of these
complexes are not from d-d transitions, but from charge-transfer from ligand
to metal orbitals (LMCT).
 Ligand to Metal Charge Transfer
• These involve excitation of an electron from a ligand-based orbital
into a d-orbital
O O
visible light
M O M O
O O
O O
• This is always possible but LMCT transitions are usually in the ultraviolet
• They occur in the visible or near-ultraviolet if
Ø metal is easily reduced (for example metal in high oxidation state)
Ø ligand is easily oxidized
If they occur in the visible or near-ultraviolet, they are much more
intense than ‘d-d’ bands and the latter will not be seen
 Ligand to Metal Charge Transfer
q They occur in the visible or near-ultraviolet if metal is easily reduced
(for example metal in high oxidation state)
TiO2 VO43- CrO42- MnO4-
Ti4+ V5+ Cr6+ Mn7+
d0 in far UV ~39500 cm-1 ~22200 cm-1 ~19000 cm-1
white white yellow purple
more easily reduced
 Coordination Complexes in Biological Systems
Porphyrins are heterocyclic macrocycles composed
of four modified interconnected pyrrole subunits.
They form coordination complexes with metal ions
and are found in biological systems.
Porphine
Chlorophyll c2 Heme B Cobalamin
 Hemoglobin and Myoglobin
Notice that the hemoglobin is essentially a tetramer of myoglobin. (There are four
myoglobin like units in hemoglobin.)
 Oxygen Binding to Myoglobin
q O2 binds to only available coordination site on iron atom.
q His 93 (proximal his) binds directly to iron.
q His 64 (distal his) stabilizes the O2 binding site.
distal histidine
proximal histidine
 Oxygen Binding Curve for Myoglobin
q Myoglobin has high 100
affinity for O2.
saturation with O2

arterial pressure
q P50 = 2.8 Torr

tissues
50
q Allows myoglobin to act
as O2 storage reserve.
q Releases O2 when pO2
becomes low indicating 2.8 20 100
O2 deprivation. pO2 (partial pressure of O2)
(Torr)
 Structural Changes in Myoglobin Upon O2 Binding
q Oxygen binding changes the Mb conformation
q Without oxygen bound, Fe is out of heme plane
q Oxygen binding pulls the Fe into the heme plane
q O2 binds to only available coordination site on iron atom.
q Fe pulls its His F8 ligand along with it
q This change means little to Mb, but lots to Hb!
 Oxygen Binding Curve for Hemoglobin
q Unlike Mb, Hb displays a sigmoidal binding curve.
q Among other things, the curve indicates that the affinity of Hb for oxygen is
lower than that of Mb!
 Physiological Significance Of O2 Binding to Hb
q Hb must be able to bind oxygen in the lungs
q Hb must be able to release oxygen in capillaries
q If Hb behaved like Mb, very little oxygen would be released in capillaries
q The sigmoid, cooperative oxygen binding curve of Hb makes this possible!
Structural Changes in Hemoglobin Upon O2 Binding
 Coordination Environment of Fe
Total unpaired electrons = 4, S = 2
Deoxygenated form is high-spin and
paramagnetic
Total unpaired electrons = 1, S = 1/2
Oxygenated form is low-spin
The magnetic moment of Fe3+ and the
superoxide radical anion involves in anti-
ferromagnetic coupling and the oxygenated
complex is not paramagnetic
 Hb and Mb in human body
More Hb More Mb
High pH Low pH
Low T High T
Low pCO2 High pCO2
The Role of the Protein
 CO binding to Mb and Hb
q Carbon monoxide is produced continuously in the body by degradation
of the porphyrin ligand (even in non-smokers).
q Under normal conditions, CO occupies approximately 1% of the heme
sites in hemoglobin and myoglobin.
q Although CO has a much greater affinity for a ferrous heme than does
O2 (by a factor of about 25,000), the affinity of CO for deoxyhemoglobin
is only about 200 times greater than that of O2, which suggests that
something in the protein is decreasing its affinity for CO by a factor of
about 100
q Both CO and NO bind to
ferrous hemes in a linear
fashion.
q In Mb and Hb, distal His
forces bent binding of
both, weakens CO binding.