Short half-life corresponds to high reactivity. The one nanosecond half-life of the hydroxyl radical indicates that it is so reactive that it reacts with the first molecule it bumps into. Ascorbate forms H2O2 on autoxidation direct combination with oxygen. Lipid peroxidation of polyunsaturated fatty acids exposed to oxygen leads to rancidity in foods.
See Article History Myoglobin, a protein found in the muscle cells of animals. It functions as an oxygen-storage unitproviding oxygen to the working muscles. Diving mammals such as seals and whales are able to remain submerged for long periods because they have greater amounts of myoglobin in their muscles than other animals do.
There is a close chemical similarity between myoglobin and hemoglobinthe oxygen-binding protein of red blood cells. Both proteins contain a molecular constituent called heme, which enables them to combine reversibly with oxygen.
The heme group, which contains ironimparts a red-brown colour to the proteins. The bond between oxygen and hemoglobin is more complex than that between oxygen and myoglobin and accounts for the dual ability hemoglobin has to transport oxygen as well as to store it.
In contact with venous blood, oxygen combines more readily with myoglobin than it does with hemoglobin, favouring the transfer of oxygen from blood to muscle cells. Thus, the oxygen that the working muscle requires for the energy-producing biochemical reactions is provided.
Myoglobin has been obtained in pure crystalline form from many sources. It has a molecular weight of 16, about one-fourth that of hemoglobin.
Though the heme portion of all myoglobins is the same, the protein portions vary considerably between species. Myoglobin has been of great importance in the elucidation of protein structure. Kendrew for work, utilizing the technique of X-ray diffractionthat permitted construction of a three-dimensional model of crystalline sperm-whale myoglobin.
Learn More in these related Britannica articles:Molecular Size and Subunit Structure of the Hemoglobins of Chironomus tentans* (Received for publication, April 26, ) exclusively monomeric with a molecular weight of approxi- mately 15, This finding was based on studies of sedi- firmation of the expected effect this chemical on molecular size of human hemoglobin, .
Dec 30, · Best Answer: I believe the last guy is right the first time. Myoglobin is a protein and has amino acids, according to Wikipedia. The average molecular weight of an amino acid is about , so you would expect the whole molecule to weigh around 17, amu (or Daltons).
16, g/mol seems like a lot, but Status: Resolved. Experimental Molecular Weight of Myoglobin Literature Molecular Weight of Myoglobin 16, Da 16, 1 Da Table 2 above displays the differences in molecular weight between the literature and experimental values of the molecular weight of myoglobin.
The molecular weight of myoglobin is 16,, which is only 25% of the total weight of hemoglobin. One myoglobin protein contains only one heme prosthetic group and therefore it can bind to a maximum of one oxygen molecule only.
Tertiary structure of protein and Anfinsen experiment. CHEM Lab Final. What method was used in Experiment 5 to determine the molecular weight of myoglobin? gel permeation chromatography. What are the other three names for GPC? The method used in this experiment could be used as a way to find sucrose concentration only if the solution was first subjected to digestion by acid .
Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.