A drop in pH would make protonation more likely, and a protonated proximal histidine would not be able to donate its electron density to the iron atom.
<h3>
What is the role of proximal histidine in hemoglobin?</h3>
The first histidine that is bonded to Fe(2+) we call proximal, and the histidine that bonds last, to the oxygen, we call distal.
Histidine is an amino acid most people get from food. It's used in growth, repair of damaged tissues, and making blood cells.
It helps protect nerve cells. It's used by the body to make histamine.
In hemoglobin, the role of proximal histidine is to hold the heme group in the correct location on the hemoglobin chain.
The proximal histidine also pulls the iron in heme out of the plane of the heme molecule. This iron will be pulled back into the plane when it is oxygenated.
The proximal histidine strengthens the iron-imidazole bond and helps to stabilize the oxidoreductase in its higher oxidation (i.e. compounds I and II) states.
To learn more about histidine, refer
brainly.com/question/14115232
#SPJ4
The answer is c i just took the test and got it right
Answer:
C. Lack of a bill of rights in the new constitution is problematic is the correct answer.
Explanation:
The Anti Federalists were the politicians who were against the US constitution which was adopted in 1787. They considered the constitution to be giving too much power to the central government and they were afraid of giving too much power to single national government as the government could infringe upon the rights of citizens and states. Patrick Henry, James Winthrop and George Mason were some of the famous Anti federalists. They were afraid of the new constitution because the states were given more power in Articles of Confederation and Perpetual Union while it wasn't so in the new constitution. Their influence led to the passage of bill of rights. They wanted to establish a weak Central government as was in Articles of Confederation and wanted for strong central governments.
