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Hemoglobin: Difference between revisions
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Heme is the prosthetic group of hemoglobin, myoglobin, and the cytochromes. It consists of a porphyrin, known as a heterocyclic ring, is located at the center of the molecule and has an [[iron]] [[atom]] bound at its center.<ref>[http://www.rpi.edu/dept/bcbp/molbiochem/MBWeb/mb2/part1/heme.htm Synthesis of Heme] Joyce J. Diwan. Biochemistry of Metabolism </ref> Globin is the [[protein]] that protects the heme molecule from any other dangers. It is also called a globular protein. A single unit of hemoglobin includes a heme that is attached to a globular protein.<ref name=bioche> [http://themedicalbiochemistrypage.org/hemoglobin-myoglobin.html Hemoglobin and Myoglobin ] Michael W. King. The Medical Biochemistry Page </ref> Hemoglobin synthesis requires the collaboration of heme and globin. In the mitochondria and the [[cytosol]] of immature red blood cells, the heme part is combined with a series of steps. On the other hand, the globin protein parts are incorporated with ribosomes in the cytosol. From the proerythroblast to the reticulocyte in the bone marrow, they keep producing hemoglobins in the cell. The nucleus is then removed from mammalian red blood cells. This happens only in humans but not in other species. Although the nucleus is disappeared in red blood cells, residual ribosomal RNA keeps combining and producing hemoglobin until the reticulocyte loses its RNA as soon as it enters the vasculature. | Heme is the prosthetic group of hemoglobin, myoglobin, and the cytochromes. It consists of a porphyrin, known as a heterocyclic ring, is located at the center of the molecule and has an [[iron]] [[atom]] bound at its center.<ref>[http://www.rpi.edu/dept/bcbp/molbiochem/MBWeb/mb2/part1/heme.htm Synthesis of Heme] Joyce J. Diwan. Biochemistry of Metabolism </ref> Globin is the [[protein]] that protects the heme molecule from any other dangers. It is also called a globular protein. A single unit of hemoglobin includes a heme that is attached to a globular protein.<ref name=bioche> [http://themedicalbiochemistrypage.org/hemoglobin-myoglobin.html Hemoglobin and Myoglobin ] Michael W. King. The Medical Biochemistry Page </ref> Hemoglobin synthesis requires the collaboration of heme and globin. In the mitochondria and the [[cytosol]] of immature red blood cells, the heme part is combined with a series of steps. On the other hand, the globin protein parts are incorporated with ribosomes in the cytosol. From the proerythroblast to the reticulocyte in the bone marrow, they keep producing hemoglobins in the cell. The nucleus is then removed from mammalian red blood cells. This happens only in humans but not in other species. Although the nucleus is disappeared in red blood cells, residual ribosomal RNA keeps combining and producing hemoglobin until the reticulocyte loses its RNA as soon as it enters the vasculature. | ||
In adult humans, hemoglobin is a tetramer, which has two alpha and two beta subunits. The subunits are identical in structure and have equal size. Each subunit has a molecular weight of 16,000 grams. Therefore, a total molecular weight is about 64,000 grams. Since each subunit of hemoglobin includes a single heme, as we aleardy discuss that a heme consists of four different molecules, adult human hemoglobin has a toatla binding capacity of four oxygen molecules. <ref name=bioche/> | In adult humans, hemoglobin is a tetramer, which has two alpha and two beta subunits. The subunits are identical in structure and have equal size. Each subunit has a [[molecular weight]] of 16,000 grams. Therefore, a total molecular weight is about 64,000 grams. Since each subunit of hemoglobin includes a single heme, as we aleardy discuss that a heme consists of four different molecules, adult human hemoglobin has a toatla binding capacity of four oxygen molecules. <ref name=bioche/> | ||
[[File:Heme.png|right|250px|thumb|Heme.]] | [[File:Heme.png|right|250px|thumb|Heme.]] | ||
