Myoglobin (Mb) is an important oxygen binding protein that stores molecular oxygen in muscle cells. It is a primarily alpha helical protein. It consists of eight helical segments that are folded into a globular structure, creating a cradle. Within this cradle lies a single heme group. The heme group contains an iron (Fe) atom at its center. Four of the ligands to this iron ion are provided by nitrogen atoms in the pyrrole ring system. The fifth ligand, on one side of the heme, is provided by a nitrogen atom from the imidazole group of His 93, also known as His F8, the eighth residue of the 'F helix' of myoglobin. The sixth ligand to iron is provided by molecular oxygen, which binds to the heme group in a pocket formed by Mb. Mb can bind only one oxygen molecule. Several residues are crucial to the function of myoglobin including Val 68 , which discriminates between various ligands and Leu 29, which influences binding and accounts for myoglobin's atypical ligand binding properties. For more information on myoglobin, consult: Bisig, D. A. et al. (1995) The Journal of Biological Chemistry 35: 20754-20762. You may wish to manipulate this image yourself: Click and hold the left mouse button to rotate the image about the x and y axes. Rotate about the z axis by pressing the shift key and right mouse button together. The image may be translated along the x and y axes by pressing control and the right mouse button. By pressing shift and the left mouse button together, you may zoom the image in or out. Clicking the right mouse button on the image gives a menu which offers several choices, including spinning the image and changing the appearance and color of the molecule.
It is a primarily alpha helical protein. It consists of eight helical segments that are folded into a globular structure, creating a cradle. Within this cradle lies a single heme group. The heme group contains an iron (Fe) atom at its center. Four of the ligands to this iron ion are provided by nitrogen atoms in the pyrrole ring system. The fifth ligand, on one side of the heme, is provided by a nitrogen atom from the imidazole group of His 93, also known as His F8, the eighth residue of the 'F helix' of myoglobin. The sixth ligand to iron is provided by molecular oxygen, which binds to the heme group in a pocket formed by Mb. Mb can bind only one oxygen molecule. Several residues are crucial to the function of myoglobin including Val 68 , which discriminates between various ligands and Leu 29, which influences binding and accounts for myoglobin's atypical ligand binding properties. For more information on myoglobin, consult: Bisig, D. A. et al. (1995) The Journal of Biological Chemistry 35: 20754-20762. You may wish to manipulate this image yourself: Click and hold the left mouse button to rotate the image about the x and y axes. Rotate about the z axis by pressing the shift key and right mouse button together. The image may be translated along the x and y axes by pressing control and the right mouse button. By pressing shift and the left mouse button together, you may zoom the image in or out. Clicking the right mouse button on the image gives a menu which offers several choices, including spinning the image and changing the appearance and color of the molecule.
Within this cradle lies a single heme group. The heme group contains an iron (Fe) atom at its center. Four of the ligands to this iron ion are provided by nitrogen atoms in the pyrrole ring system. The fifth ligand, on one side of the heme, is provided by a nitrogen atom from the imidazole group of His 93, also known as His F8, the eighth residue of the 'F helix' of myoglobin. The sixth ligand to iron is provided by molecular oxygen, which binds to the heme group in a pocket formed by Mb. Mb can bind only one oxygen molecule. Several residues are crucial to the function of myoglobin including Val 68 , which discriminates between various ligands and Leu 29, which influences binding and accounts for myoglobin's atypical ligand binding properties. For more information on myoglobin, consult: Bisig, D. A. et al. (1995) The Journal of Biological Chemistry 35: 20754-20762. You may wish to manipulate this image yourself: Click and hold the left mouse button to rotate the image about the x and y axes. Rotate about the z axis by pressing the shift key and right mouse button together. The image may be translated along the x and y axes by pressing control and the right mouse button. By pressing shift and the left mouse button together, you may zoom the image in or out. Clicking the right mouse button on the image gives a menu which offers several choices, including spinning the image and changing the appearance and color of the molecule.
The heme group contains an iron (Fe) atom at its center. Four of the ligands to this iron ion are provided by nitrogen atoms in the pyrrole ring system. The fifth ligand, on one side of the heme, is provided by a nitrogen atom from the imidazole group of His 93, also known as His F8, the eighth residue of the 'F helix' of myoglobin. The sixth ligand to iron is provided by molecular oxygen, which binds to the heme group in a pocket formed by Mb. Mb can bind only one oxygen molecule. Several residues are crucial to the function of myoglobin including Val 68 , which discriminates between various ligands and Leu 29, which influences binding and accounts for myoglobin's atypical ligand binding properties. For more information on myoglobin, consult: Bisig, D. A. et al. (1995) The Journal of Biological Chemistry 35: 20754-20762. You may wish to manipulate this image yourself: Click and hold the left mouse button to rotate the image about the x and y axes. Rotate about the z axis by pressing the shift key and right mouse button together. The image may be translated along the x and y axes by pressing control and the right mouse button. By pressing shift and the left mouse button together, you may zoom the image in or out. Clicking the right mouse button on the image gives a menu which offers several choices, including spinning the image and changing the appearance and color of the molecule.
Several residues are crucial to the function of myoglobin including Val 68 , which discriminates between various ligands and Leu 29, which influences binding and accounts for myoglobin's atypical ligand binding properties. For more information on myoglobin, consult: Bisig, D. A. et al. (1995) The Journal of Biological Chemistry 35: 20754-20762. You may wish to manipulate this image yourself: Click and hold the left mouse button to rotate the image about the x and y axes. Rotate about the z axis by pressing the shift key and right mouse button together. The image may be translated along the x and y axes by pressing control and the right mouse button. By pressing shift and the left mouse button together, you may zoom the image in or out. Clicking the right mouse button on the image gives a menu which offers several choices, including spinning the image and changing the appearance and color of the molecule.
For more information on myoglobin, consult: Bisig, D. A. et al. (1995) The Journal of Biological Chemistry 35: 20754-20762.
You may wish to manipulate this image yourself: