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What is the site of oxygen binding on hemoglobin?
You have Iron atoms in hemoglobin. This atom is the binding site for oxygen in case of hemoglobin.
What is it orderless colorless gas which binds preferentially with the same binding site on hemoglobin?
The orderless, colorless gas that binds preferentially with the same binding site on hemoglobin is carbon monoxide (CO). It competes with oxygen for binding to hemoglobin, forming carboxyhemoglobin, which reduces the blood's ability to carry oxygen and can lead to oxygen deprivation in tissues. This property makes carbon monoxide particularly dangerous in enclosed spaces where it can accumulate.
Does carbon monoxide compete with oxygen for the same binding site?
Yes. Carbon monoxide combines with haemoglobin to form carboxyhaemoglobin. This prevents the normal combination of oxygen with haemoglobin, thus depriving cells all round the body of the oxygen they need.
What binding site does carbon monoxide has?
Carbon monoxide has a high affinity for the heme group in hemoglobin, binding to the iron atom in place of oxygen. This prevents oxygen from binding, reducing the blood's ability to transport oxygen to tissues, leading to tissue hypoxia.
What inhibitor has a structure similar to the substrate?
Competitive inhibitors have a structure similar to the substrate, allowing them to bind to the active site of the enzyme and block the substrate from binding. This competition for the active site reduces the enzyme's catalytic activity by preventing the substrate from binding and undergoing a reaction.
What is the site of oxygen binding on hemoglobin?
You have Iron atoms in hemoglobin. This atom is the binding site for oxygen in case of hemoglobin.
What portion of hemoglobin molecule binds oxygen?
Hemoglobin contains a heme group with an Iron ion attached to it. The iron is what binds to O2.
Does CO2 bind at the same site on the hemoglobin molecule as O2 If not where does CO2 bind?
No. Carbon monoxide binds to the same site as oxygen, i.e. the central iron. Carbon dioxide binds to the globin molecule.
What is the region on an enzyme to which a substrate bind is called?
Binding site.
Where is the binding site for oxygen in the body?
Hemoglobin on red blood cells.
Do uncompetitive inhibitors bind to the active site of enzymes?
No, uncompetitive inhibitors do not bind to the active site of enzymes. They bind to a different site on the enzyme, causing a conformational change that prevents the substrate from binding to the active site.
Do competitive inhibitors bind to the active site of enzymes?
Competitive inhibitors bind to the active site of enzymes, blocking the substrate from binding and inhibiting the enzyme's activity.
How are the different types of inhibitors different?
Competitive inhibitors bind to the active site of an enzyme, preventing the substrate from binding. Noncompetitive inhibitors bind to a site other than the active site, changing the shape of the enzyme and preventing substrate binding. Uncompetitive inhibitors bind only to the enzyme-substrate complex, preventing catalysis.
Does carbon monoxide compete with oxygen for the same binding site?
Yes. Carbon monoxide combines with haemoglobin to form carboxyhaemoglobin. This prevents the normal combination of oxygen with haemoglobin, thus depriving cells all round the body of the oxygen they need.
Where do non-competitive inhibitors bind in relation to the enzyme's active site?
Non-competitive inhibitors bind to a site on the enzyme that is not the active site, causing a change in the enzyme's shape and preventing the substrate from binding effectively.
What requires a binding site called palindrome?
DNA polymerase requires a binding site called palindrome. This binding site allows the enzyme to recognize and bind to specific sequences on the DNA strand in a complementary manner, ensuring accurate copying of genetic information during DNA replication. Palindromic sequences are characterized by their two-fold symmetry, which aids in DNA polymerase's ability to bind and initiate replication.
How do noncompetitive and allosteric inhibitors differ in their mechanisms of action on enzymes?
Noncompetitive inhibitors bind to a site on the enzyme that is not the active site, causing a change in the enzyme's shape and preventing substrate binding. Allosteric inhibitors bind to a different site on the enzyme, causing a conformational change that affects the active site's ability to bind substrate.
