The isolated iron–molybdenum cofactor of nitrogenase binds carbon monoxide upon electrochemically accessing reduced states

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Abstract
The first spectroscopic evidence for the binding of a small gaseous molecule to the isolated iron molybdenum cofactor of nitrogenase (FeMoco) is presented: FTIR spectroelectrochemistry in a thin-layer cell shows that reduced FeMoco binds carbon monoxide and gives rise to ν(CO) stretches that are close to those observed during turnover of the enzyme.

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