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Hemoglobin (Carbon Monoxide Binding (Homotropic effectors, Binds…

Hemoglobin (Carbon Monoxide Binding , Protein Function , Histidine residue , Tense state, Bingind of oxygen ,

Fetal hemoglobin has a higher affinity than adult hemoglobin.

, Heme and globin component , Succynl-CoA is required for heme biosynthesis , 6 Coordination sites , After binding to 6th site the oxygen becomes smaller. Iron moves to the plane of porhyrin. , Relaxed conformation. After Oxygen binds there is positive cooperative of oxygen. , Hydrogen bond and salt bridges make the hemoglobin stable , 2,3 bisphosphoglycerate, Blood Oxygen , Relaxed state , Extrapulmonary tissue , Lungs , Bore effect , Band 3 )

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Hemoglobin

Hemoglobin

Protein Function

Fetal hemoglobin has a higher affinity than adult hemoglobin.

Bingind of oxygen

Carbon Monoxide Binding

Structure of hemoglobin

Has 4 polypeptides (2 alpha chains and 2 beta chains)
Has cooperativity (during loading and unloading)
Has higher oxygen carrying capacity than myoglobin

Myoglobin

has 1 polypeptide

Heme and globin component

Succynl-CoA is required for heme biosynthesis

Histidine residue

6 Coordination sites

Distal

Proximal

After binding to 6th site the oxygen becomes smaller. Iron moves to the plane of porhyrin.

Relaxed conformation. After Oxygen binds there is positive cooperative of oxygen.

Homotropic effectors

Binds perpendicularly

Distal histidine reduces binding of carbon monoxide

Binding is reversible

Example of competitive antagonism

Tense state

Deoxy state

Low affinity for Oxygen

Hydrogen bond and salt bridges make the hemoglobin stable

Binding of one Oxygen enhances the binding of the oxygen to other 3 subunit

2,3 bisphosphoglycerate

Blood Oxygen

Relaxed state

Extrapulmonary tissue

Lungs

Bore effect

Band 3