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• W2127184963 startingPage "1075" @default.
• W2127184963 abstract "It was recently suggested that electron flow into cyt c, coupled with ROS generation, oxidizes cyt c Met80 to Met80 sulfoxide (Met-O) in isolated hearts after ischemia–reperfusion, and converts cyt c to a peroxidase. We hypothesize that ischemia disrupts Met80-Fe ligation of cyt c, forming pentacoordinated heme Fe2 +, which inhibits electron transport (ET) and promotes oxygenase activity. SS-20 (Phe-D-Arg-Phe-Lys-NH2) was used to demonstrate the role of Met80-Fe ligation in ischemia. Mitochondria were isolated from ischemic rat kidneys to determine sites of respiratory inhibition. Mitochondrial cyt c and cyt c Met-O were quantified by western blot, and cristae architecture was examined by electron microscopy. Biochemical and structural studies showed that SS-20 selectively targets cardiolipin (CL) and protects Met80-Fe ligation in cyt c. Ischemic mitochondria showed 17-fold increase in Met-O cyt c, and dramatic cristaeolysis. Loss of cyt c was associated with proteolytic degradation of OPA1. Ischemia significantly inhibited ET initiated by direct reduction of cyt c and coupled respiration. All changes were prevented by SS-20. Our results show that ischemia disrupts the Met80-Fe ligation of cyt c resulting in the formation of a globin-like pentacoordinated heme Fe2 + that inhibits ET, and converts cyt c into an oxygenase to cause CL peroxidation and proteolytic degradation of OPA1, resulting in cyt c release. Cyt c heme structure represents a novel target for minimizing ischemic injury. SS-20, which we show to selectively target CL and protect the Met80-Fe ligation, minimizes ischemic injury and promotes ATP recovery." @default.
• W2127184963 created "2016-06-24" @default.
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• W2127184963 date "2015-10-01" @default.
• W2127184963 modified "2023-10-13" @default.
• W2127184963 title "Disruption of cytochrome c heme coordination is responsible for mitochondrial injury during ischemia" @default.
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• W2127184963 doi "https://doi.org/10.1016/j.bbabio.2015.06.006" @default.
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