Biochemistry 8 PDF - Globular Proteins, Hemoglobin and Myoglobin

Biochemistry 8 Globular Proteins. Structure and function of hemoglobin and myoglobin. Bohr effect. Hemoglobinopathies. Textbook - Lippincott Illustrated Reviews Biochemistry, 8th edition, 2021 Chapter 3 - ”Globular Proteins” Pages: 58-89 Topics 1. which have to b...

Biochemistry 8 Globular Proteins. Structure and function of hemoglobin and myoglobin. Bohr effect. Hemoglobinopathies. Textbook - Lippincott Illustrated Reviews Biochemistry, 8th edition, 2021 Chapter 3 - ”Globular Proteins” Pages: 58-89 Topics 1. which have to be learned Globular hemeproteins 2.Myoglobin structure and function 3.Hemoglobin structure and function 4.Oxygen-dissociation curve and Bohr effect 5.Hemoglobinopathies (HbS, HbC, HbSC, alpha and beta thalassemias)  The O2 affinity of Hb is inversely proportional to the CO2 content and H+ concentration of blood. High CO2 and H+ concentrations (from tissue metabolism) cause decreased affinity for O2 → O2 that is bound to Hb is released to tissue (the O2-Hb dissociation curve is shifted to the right). HbO2 + H+ ⇄ H+Hb + O2 HbO2 + CO2 ⇄ Hb-COO- + H+ + O2 Haldane effect The CO2 affinity of Hb is inversely proportional to the oxygenation of Hb. When Hb is deoxygenated (typically in peripheral tissue), uptake of CO2 is facilitated. When Hb is oxygenated (in high pO2, for example, in the lungs): Oxygenated Hb has a decreased affinity for CO2 → CO2 that is bound to Hb is released in the pulmonary arteries to diffuse into the alveoli (the O2-Hb dissociation curve is shifted to the left). Hb releases bound H+ → ↑ H+ shifts equilibrium to CO2 production (see equation above) → CO2 is exhaled in lungs