Tyrosine phosphorylation turns alkaline transition into a biologically relevant process and makes human cytochrome c behave as an anti-apoptotic switch

  title={Tyrosine phosphorylation turns alkaline transition into a biologically relevant process and makes human cytochrome c behave as an anti-apoptotic switch},
  author={Jos{\'e} Manuel Garc{\'i}a-Heredia and Antonio D{\'i}az-Quintana and Maria Salzano and Mar Orz{\'a}ez and Enrique Pérez-Payá and Miguel Teixeira and Miguel A. Rosa and Irene D{\'i}az-Moreno},
  journal={JBIC Journal of Biological Inorganic Chemistry},
Cytochrome c (Cc) is a key protein in cell life (respiration) and cell death (apoptosis). On the one hand, it serves as a mitochondrial redox carrier, transferring electrons between the membrane-embedded complexes III and IV. On the other hand, it acts as a cytoplasmic apoptosis-triggering agent, forming the apoptosome with apoptosis protease-activating factor-1 (Apaf-1) and activating the caspase cascade. The two functions of cytochrome c are finely tuned by the phosphorylation of tyrosines… 

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In vivo phosphorylated Cyt c shows enhanced sigmoidal kinetics with COX, and half-maximal turnover is observed at a CyT c substrate concentration of 5.5 microM compared to 2.5microM for alkaline phosphatase-treated Cytc, while Spectral analysis revealed that the characteristic 695 nm absorption band is shifted to 687 nm and reversed after treatment with alkalineosphatase.

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