Computer modelling which shows on a molecular level the reaction of a monolysocardiolipin with cytochrome c, which results in breaking the bond between iron from the hem group and metionin 80 (M80) and the transition of cytochrome to pentacoordiation form (IMAGE)

Nicolaus Copernicus University in Torun

Computer modelling which shows on a molecular level the reaction of a monolysocardiolipin with cytochrome c, which results in breaking the bond between iron from the hem group and metionin 80 (M80) and the transition of cytochrome to pentacoordiation form

Caption

Computer modelling which shows on a molecular level the reaction of a monolysocardiolipin with cytochrome c, which results in breaking the bond between iron from the hem group and metionin 80 (M80) and the transition of cytochrome to pentacoordiation form, activating at the same time an abnormal function of the protein, which is the capability of peroxidation of polyunsaturated fatty acids (PUFA).

In addition (in blue) there are lysines, amino acids with positive charge, which allow the cytochrome C to join the lipid membrane (in orange)

Credit

Karolina Mikulska-Ruminska, NCU

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