Pitt BIOSC 1000 - Protein Function: Myoglobin and Hemoglobin (9 pages)

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Protein Function: Myoglobin and Hemoglobin



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Protein Function: Myoglobin and Hemoglobin

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This lecture introduces the functions of protein, myoglobin, hemoglobin, and the interactions between hemoglobin and binding molecules.


Lecture number:
6
Pages:
9
Type:
Lecture Note
School:
University of Pittsburgh
Course:
Biosc 1000 - Biochemistry

Unformatted text preview:

BIOSC 1000 Lecture 6 Outline of Previous Lecture 1 Protein Structure Review 2 Protein Purification Outline of Current Lecture 1 Protein Function Myoglobin Hemoglobin 2 Hemoglobin 3 BPG Binding to Hb Current Lecture 1 Protein Function Myoglobin Hemoglobin Oxygen is required for aerobic metabolism of fuel Delivery of oxygen is limited by its scarce solubility in water o 0 1 mM in blood plasma VERY low Blood comprised of plasma 55 and mixture of cells 45 Cellular elements Cellular Elements o Cells or descendants from cells o White blood cells o Red blood cells 6 m small cells Filled with hemoglobin and metabolic enzymes Lack nuclei and other organelles o Platelets derived from cells Solution specific protein to carry O2 in the blood In essence hemoglobin helps O2 dissolve in blood Whole blood has 150g of hemoglobin L and Hb carries concentrations as high as 10mM O2 100fold higher than O2 solubility Myoglobin occurs in cells that use large amounts of oxygen particularly muscle Mb represents O2 storage o 1 peptide chain functions as a monomer o 1 heme group binds 1 O2 1 per heme o Mb 153 AA Mr 16 700 HbA 4 polypeptide chains alpha2 beta2 o Each like Mb in sequence and 3 structure o 4 heme groups 1 per chain binds up to 4 O2 1 heme o alpha Hb 141AA Mr 15 100 o beta Hb 146 AA Mr 15 900 Heme group of myoglobin and hemoglobin o Heme comprised of four pyrrole rings liked by methane bridges also called porphyrin plus one metal ion prosthetic group o Free heme binds strongly to molecular oxygen and oxygen oxidizes Fe2 to Fe3 o Center of molecule o Prosthetic Group a compound that is permanently associated with a protein and contributes to the usual function of the protein o Venous blood deoxygenated hemoglobin dark purplish hue o Arterial blood oxygenated hemoglobin bright red Change in spectral properties of heme oxygen changes color o Heme oxygen red Oxygen binding to Myoglobin Heme o Histidine 93 touches Fe o H 64 too far away to form a bond with Fe but if an Oxygen comes in



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