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Regulation of O2 binding
and release
1
Structure is key to function
Myoglobin: monomeric
Hemoglobin: tetrameric,
each chain resembles
myoglobin
How can nearly identical
structures perform such
different functions
(storage versus
transport)?
Mb + O2 MbO2
Ma per
K = [MbO2]/[Mb][O2]
quindi [MbO2]= K [Mb][O2]
= 0.5 (50% Mb legata allO2)
22 in urea gives 2
suggesting strong
interactions between
rather than and
X-ray diffraction has
showed that in fact the DEOXY OXY
dimer rotates and slides
with respect to one
another narrowing the
central cavity;
This is consistent with the
R and T states
Prof. G. Gilardi - Biological Chemistry
Molecular details:
Deoxy form:
The C-ter. of 2 (res. 146) lies on top of the C-
ter. helix of 1
Note that here the release of H+ furher helps in the Bohr effect;
It follows that CO2 transport stimulates O2 release: for
this reason hyperventilation, breathing too rapidly with
excess release of CO2 leads to dizziness and
unconsciousness; this can be easily corrected by
breathing into a paper bag to bring up the level of CO2
Prof. G. Gilardi - Biological Chemistry
Biphosphoglycerate - BPG