In the Bohr effect, protonation of the imidazolium rings of the C-terminal rings of the C-terminal residues (His 126B) of the hemoglobin's two B chains is responsible for around 40% of the .60 mole of H+ that combine with Hb on the release of 1.00 mole of O2 at pH 7.40. Assuming that this imidazolium group has pKa = 7.10 in R-state oxyHb, what is its pKa value in T-state deoxyHb? (Hint: the pH of the blood - because it's buffered - doesn't change when going from R-state oxyHb to T-state deoxyHb)... Also please note that this is really a biochemistry problem, but i'm desperate if anyone has ANY idea how to even start this problem. Thanks in advance!
I am giving an idea to solve this problem, not solution as per your request.
At a given pH, the contribution of each hydrogen ion binding
site to the total number of Bohr protons that can be additionally
bound in deoxyHb is determined by the magnitude of the
deoxygenation induced increase in pKa, and the closeness of the pKa
values in oxy and deoxy Hb to the given pH. The individual
contribution of a Bohr siteH+
i is given by two times the difference in fractional occupation of
the hydrogen ion binding site between T-state deoxyHb and R-state
oxyHb:
where KTai and KRai are the acid dissociation constants of an individual (i) site in T-state and R-state Hb, respectively.
R state ("oxy" conformation, high O2 binding affinity) stabilized by O2 binding (O2 is a homotropic effector) T state ("deoxy" conformation, low O2 binding affinity) stabilized by binding of protons (H+) , CO2, and/or 2,3- bisphosphoglycerate (2,3-BPG) (all heterotropic effectors)
I would like to suggest you to please go through the following journal for more information
Evolution of vertebrate haemoglobins: Histidine side chains,specific buffer value and Bohr effect - Title of journal
Respiratory Physiology & Neurobiology 154 (2006) 165–184
or download pdf by copy paste below one exactly in google search engine and download 1st link
ΕΞΕΛΙΞΗ ΤΗς ΑΙΜΟΣΦΑΙΡΙΝΗΣ.pdf
Thank you
In the Bohr effect, protonation of the imidazolium rings of the C-terminal rings of the C-terminal...
In the Bohr effect, the protonation of the N-terminal amino groups in the alpha chains of hemoglobin is responsible for 30% of the 0.6moles of H+ that combine with hemoglobin when 1 mole of O2 is released at pH 7.4. Assuming that the N-terminial amino groups have a pKeq of 7.0 in the R state, what is the pKeq in the T state?
The Bohr Effect results in the release of protons when O2 binds to Hb. The beta subunit of Hb possesses a terminal histidine with a pka of 7.1 in the T state. What is the ratio of protonated to unprotonated histidine at pH 7.4? When the conformation of Hb changes to the R state, does the pka of the histidine increase or decrease? What would cause this change in pka?
Respiratory alkalosis leads to a shift of hemoglobin to the active R state. At first, it may be unclear why shifting to the R state is a bad thing, but the reason should be clear shortly. First, let us examine how CO, also affects hemoglobin directly. CO2 has a direct effect on hemoglobin In addition to its indirect effect on hemoglobin structure through its effect on pH, CO, also directly affects hemoglobin by reacting with the amino-terminal residue of each...