'Oxygen binding' diaporamas de présentation

About this Chapter

About this Chapter. Diffusion and solubility of gases Gas exchange in lungs and tissues Gas transport in the blood Regulation of ventilation. Overview. O 2. CO 2. Airways. Alveoli of lungs. O 2. CO 2. 6. CO 2 exchange at alveolar-capillary interface. Oxygen exchange

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Myoglobin

1. 2. Myoglobin. Heme. 3. 4. Hemoglobin (Hb) functions to transport oxygen in the blood of all warm-blooded animals. It is a multimeric protein consisting of

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Regulatory Strategies: ATCase & Haemoglobin

Regulatory Strategies: ATCase & Haemoglobin. Aspartate transcarbamolase is allosterically inhibited by the end product of its pathway. Carbamoyl phosphate + aspartate ? N-carbamoylaspartate + Pi. Aspartate transcarbamolase.

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Globins

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Gas Exchange and Transport

Gas Exchange and Transport. 18. Overview. O 2. CO 2. Airways. Alveoli of lungs. O 2. CO 2. 6. CO 2 exchange at alveolar-capillary interface. Oxygen exchange at alveolar-capillary interface. 1. O 2. CO 2. Pulmonary circulation. Oxygen transport. 2. 5. CO 2 transport.

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Biochemistry

Biochemistry. Robert F. Waters PhD. Porphyrin Rings. Produced mainly in: Liver Erythrocyte producing cells of bone marrow Not mature erythrocytes (lack of mitochondria) Initial step and last three steps are in the mitochondria Glycine and Succinyl CoA are precursors

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Structures of Myoglobin and Hemoglobin

Structures of Myoglobin and Hemoglobin. Myoglobin ( Mb ) - monomeric protein that facilitates the diffusion of oxygen in vertebrates Hemoglobin ( Hb ) - tetrameric protein that carries oxygen in the blood

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Structures of Myoglobin and Hemoglobin

Structures of Myoglobin and Hemoglobin. Myoglobin ( Mb ) - monomeric protein that facilitates the diffusion of oxygen in vertebrates Hemoglobin ( Hb ) - tetrameric protein that carries oxygen in the blood

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Hemoglobin

Deepa John Harini Chandra. Hemoglobin.

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Chapter 5.1: Protein Function - Reversible Binding of Protein to a Ligand

Chapter 5.1: Protein Function - Reversible Binding of Protein to a Ligand. CHEM 7784 Biochemistry Professor Bensley. CHAPTER 5.1 Reversible Binding of Protein to a Ligand. Reversible binding of ligands Structure of myoglobin and hemoglobin Origin of cooperativity in hemoglobin.

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Protein Function

Protein Function. Structure will determine the function of the protein. Key ideas and terms. protein can bind a ligand in the binding site For an enzyme, the ligand is a substrate and they bind in what is called the active site ligand has to be the correct shape

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Dental Biochemistry Lectures 39 and 40 2014 HEME AND HEMOGLOBIN

Dental Biochemistry Lectures 39 and 40 2014 HEME AND HEMOGLOBIN. Michael Lea. Porphyrins and Hemoglobin - Lecture Outline. 1. Synthesis of Porphyrins 2. Regulation of Heme synthesis 3. Porphyrias 4. Degradation of Heme and Jaundice 5. Hemoglobin Structure and Function

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Biochemistry Teachable Unit

Biochemistry Teachable Unit. Junior/senior course in Biology or Biochemistry. Teachable Unit for 2 class periods. Background knowledge: general biology and general chemistry. Prior knowledge: fundamental protein structure from amino acids through quaternary structure. Learning Goals

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Myoglobin and hemoglobin

Myoglobin and hemoglobin. Lecture 11 Modified from internet resources, books and journals. Myoglobin and hemoglobin. hemeproteins physiological importance ? bind molecular oxygen Myoglobin ? in muscle tissue where it serves as an intracellular storage site for oxygen

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Temperature Controlled Rate Studies of Co(salen) Reversible Oxygen Binding

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Globular Proteins

Globular Proteins. Some design principles Globular proteins fold so as to "bury" the hydrophobic side chains, minimizing their contact with water Most polar residues face the outside of the protein and interact with solvent

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Temperature Controlled Rate Studies of Co(salen) Reversible Oxygen Binding

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Structure

Structure. Hemoglobin. Tetramer of a 2 b 2 Each subunit binds one heme Oxygen transporter in RBCs. Myoglobin. Monomer with one heme Oxygen reservoir in muscle. Heme. Fe 2+ bound to center of protoporphyrin IX. Structural Changes To Hemo-globin From Oxygen Binding.

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Extra credit

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Hemoglobin: Quaternary Structure

Hemoglobin: Quaternary Structure. Heme Group. Oxygen Binding to Hemoglobin: Conformational Change. deoxyhemoglobin. oxyhemoglobin. oxygen release. % saturation. tissues. lungs. Oxygen Binding to Hemoglobin. pH 7.6. pH 6.8. lungs. tissues. Hemoglobin-Oxygen Binding Equilibrium.

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