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Aerobic respiration: Proof of concept for the oxygen-centric murburn perspective.

The inner mitochondrial membrane protein Complexes (I - V) and prokaryotic respiratory machinery are examined for a deeper understanding of their structure-function correlations and dynamics. In silico analysis of the structure of complexes I-IV, docking studies and erstwhile literature confirm that they carry ADP binding sites which are in close proximity to DROS (diffusible reactive oxygen species) generating redox centers. These findings provide supportive evidence for the newly proposed oxygen-centric chemical-coupling mechanism (murburn concept), wherein DROS catalyzes the esterification of inorganic phosphate to ADP. Further, in a reductionist system, we demonstrate that a DROS like superoxide can effectively esterify inorganic phosphate to ADP. The impact of these findings and the interactive dynamics of classical inhibitors (rotenone & cyanide), uncouplers (dinitrophenol & uncoupling protein) and other toxins (atractyloside & oligomycin) are briefly discussed.

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