Cytochrome C -Adis: Difference between revisions
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cysteine residues. This heme prosthetic is four cyclic structures forming a circle around a central | cysteine residues. This heme prosthetic is four cyclic structures forming a circle around a central | ||
iron atom. They can form different compounds by having different attachments around the 4 | iron atom. They can form different compounds by having different attachments around the 4 | ||
pyrrole rings. Two conformations of cytochrome C exist naturally. In the monoheme | pyrrole rings. Two conformations of cytochrome C exist naturally but both having the same general <scene name='Sandbox_Reserved_335/Motif/1'>structure</scene>. In the monoheme | ||
form, the other axial position is usually left empty however, it can be occupied by other | form, the other axial position is usually left empty however, it can be occupied by other | ||
molecules such as histidine or lysine. Leaving the location empty prevents steric hindrance and | molecules such as histidine or lysine. Leaving the location empty prevents steric hindrance and | ||