Elucidating the mechanism of

Mo-dependent nitrogenase consists of two subunits, the Fe protein, a homodimer, and the Mo Fe protein, an ).

The promise of exponential speedups for the electronic structure problem has led many to suspect that quantum computers will one day revolutionize chemistry and materials science. Not the least of these is the question of how exactly to use a quantum computer to solve an important problem in chemistry.Here, we show how quantum computers can be used to elucidate the reaction mechanism for biological nitrogen fixation in nitrogenase, by augmenting classical calculation of reaction mechanisms with reliable estimates for relative and activation energies that are beyond the reach of traditional methods.We also show that, taking into account overheads of quantum error correction and gate synthesis, a modular architecture for parallel quantum computers can perform such calculations with components of reasonable complexity.This enzyme accomplishes the remarkable transformation of dinitrogen into two ammonia molecules under ambient conditions.Whereas the industrial Haber–Bosch catalyst requires high temperature and pressure and is therefore energy-intensive, the active site of Mo-dependent nitrogenase, the iron molybdenum cofactor (Fe Moco) (23, 24), can split the dinitrogen triple bond at room temperature and standard pressure.Experiments have not yet been able to provide sufficient details on the chemical mechanism, and theoretical attempts are hampered by intrinsic methodological limitations of traditional quantum chemical methods.

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