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Bioinorganic Chemistry

Chapter 16
Bioinorganic Chemistry
Only a few representative examples will be
presented for these bioinorganic compounds
and their actions.
Table 16-1 (mammalian biochemistry)
Examine the importance of iron.
A relatively new area of study for bioinorganic
molecules is the incorporation of MO
calculations.
Porphyrins and Related Complexes
in Bioinorganic Molecules
A porphine ring has a square planar geometry with a
pocket in the center.
Examine Fig. 16-1.
A metalloporphyrin complex can result by
incorporating a metal atom into the pocket (look at
heme from Rasmol).
Axial sites are available for other ligands.
Structure, specificity, and reactivity are changed by
differing the side chains, metal ions, and surrounding
species.
Hemoglobin and Myoglobin
Oxygen transfer and storage agents in the
blood and muscle tissue.
Hemoglobin transports oxygen (O2) from the
lungs/gills to tissues and muscles.
Myoglobin stores oxygen (O2) in the muscles
and tissues.
Oxygen commonly transfers from the hemoglobin
to the myoglobin for later use.
Hemoglobin
Made up of four globin protein subunits ( and ).
Each protein partially encloses a heme group.
Each heme group is in a porphyrin pocket.
One axial position of the iron is bound to an imidazole
nitrogen from the protein.
One axial position is available/vacant or has H2O bound
to it.
Dissolved O2 can bind reversibly to this axial position.
http://www.umass.edu/microbio/chime/hemoglob/
Hemoglobin
In hemoglobin, the Fe(II) does not become
oxidized to Fe(III) or Fe(IV).
Occurs readily in simpler systems (see Figure on the
next page).
There needs to be reversible binding of the O2
without oxidation. A free heme also oxidizes in
an aqueous environment.
Why doesnt oxidation occur in hemoglobin by O2 or
H2O?
Hemoglobin (Figures)
Hemoglobin
In nonoxygenated hemoglobin, the Fe(II) is about
70 pm out of the plane of the porphyrin nitrogens
(show with Chime).
Bonding O2 or CO in the sixth position causes the
iron to be come planar.
Fe(II) becomes diamagnetic
Oxygen bonds at an angle of ~130 degrees (show
with Chime).
Explain these structural changes upon bonding.
Hemoglobin
There is a considerable amount of
backbonding from the metal to the O2.
Can be described as Fe(III)-O2-
Why is the O2 bent? The energy changes
very little with this angle.
suggestions
Hemoglobin
Cooperativity
The function of hemoglobin is to bind O 2 at high oxygen
pressure and carry it through the blood to needed areas
(and myoglobin for storage).
Hb + 4O2 Hb(O2)4
Hb(O2)4 + 4Mb 4Mb(O2) + Hb
As one iron binds an oxygen molecule in Hb, the
molecular shape changes to make binding of
additional oxygen molecules easier. In a similar
fashion, initial removal of oxygen triggers the release
of the remaining oxygens.
Hemoglobin
At low partial pressures of
O2, Mb has a much greater
affinity for O2.
[Mb(O 2 )]
K Mb
[Mb][O 2 ]

[Hb(O 2 ) 4 ]
K Hb
[Hb][O 2 ]2.8
The Bohr effect.
Increased acidity favors the
release of O2 from Hb(O2)4