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Photosynthetic organisms have been optimized by over two billion years of evolution into energy-harvesting machines that surpass the efficiency of man-made solar devices. Employing a network of hundreds of proteins, these organisms transform energy from the incident sunlight into ATP molecules - the universal fuel for sustaining cellular activities. A key step in the conversion of solar energy into ATP involves shuttling of negative charges or electrons between widely separated sites on the cell membrane. This membrane-wide charge transportation is accomplished by the cytochrome c family of proteins. Cytochrome c finds and docks to an electron donor protein, accepts the electron and unbinds as a result of it, and afterwards finds an electron acceptor protein, docks to it to deliver the electron and unbinds to repeat the sequence. Given its ubiquitous role in photosynthesis and respiration, the recognition, binding and unbinding mechanism of cytochrome c have been a focus of intense biochemical investigations over the past three decades. However, little is deciphered on the details of cytochrome c activity. A recent study based on molecular dynamics simulations with NAMD reveals the working principles of cytochrome c in atomic resolution. The calculations suggest that electrostatic forces drive the cytochrome c binding, and enable membrane-wide electron transfer. More about the cytochrome c protein can be found here.