Beruflich Dokumente
Kultur Dokumente
Hemoglobin
Spherical 64 x 55 x 50 two fold rotation of
symmetry and subunits are similar and are placed
on the vertices of a tetrahedron. There is no D helix in
the chain of hemoglobin. Extensive interactions
between unlike subunits 2-2 or 1-1 interface
has 35 residues while 1-2 and 2-1 have 19
residue contact.
T-state
R-state
Hemoglobin function
2,2 dimer which are structurally similar to myoglobin
Transports oxygen from lungs to tissues.
O2 diffusion alone is too poor for transport in larger
animals.
Solubility of O2 is low in plasma i.e. 10-4 M.
But bound to hemoglobin, [O2] = 0.01 M or that of air
Two alternative O2 transporters are;
Hemocyanin, a Cu containing protein.
Hemoerythrin , a non-heme containing protein.
Binding of oxygen
rearranges the electronic
distribution and alters the d
orbital energy.
This causes a difference in
the absorption spectra.
Bluish for deoxy Hb
Redish for Oxy Hb
Measuring the absorption at
578 nM allows an easy
method to determine the
percent of Oxygen bound to
hemoglobin.
O2 binding to myoglobin
Mb O 2
[Mb][O 2 ]
Kd
[MbO 2 ]
Fractional Saturation solve for [MbO2] and plug in
[MbO 2 ]
[O 2 ]
YO 2
[Mb] [MbO 2 ] Kd [O 2 ]
pO 2
YO 2
K d pO 2
pO 2
YO 2
P50 pO 2
What does the value of P50 tell you about the O2 binding
affinity?
E nS ESn
O2 is considered a ligand
n
[E][S]
1. K
[ESn]
n[ESn]
2. Ys
n [E] [ESn]
[E][S]
K
Ys
n
1 [S]
[E]
K
3.
or
[S]
Ys
n
K [S]
Continuing as before:
K P50
pO 2
n
n
P50 pO 2
n
4.
YO 2
n = 1, non-cooperative
n < 1, negative cooperativity
Hill Plot
Rearrange equation 4.
Ys
Log
nLog[S] logK
1 - Ys
y
mx
Things to remember
0.55 at 30 torr
a YO2 of 0.40
Understand Fig 9-3
Fe O
O Fe
Hb O 2 n H x O 2 Hb O 2 n 1 xH
CO 2 H 2 O H HCO 3
Lecture 3/12/2003
Protein Function II
Globins and Antibodies