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S 2B or not 2B?
1School of Chemistry, UNSW Sydney, NSW 2052, Australia. i.dance@unsw.edu.au.
Abstract:
In recent years a large collection of experimental information has prompted proposals that an atom, S2B, part of the catalytic metal cluster FeMo-co of the enzyme nitrogenase, is displaced during the enzyme mechanism in order to allow the binding of substrate N2 to the adjacent Fe atoms. Computational investigation has generated a complete enzyme mechanism in which S2B is retained in its resting state position, and as such is an essential agent in the enzyme mechanism. A dilemma arises, between a disruptive mechanism - with S2B moved out of the way during the reaction steps - and a conservative mechanism - with S2B retained and necessarily used. Following the Prince of Denmark, is the 2B position of FeMo-co to be S or not to be S? I have assembled the evidence and arguments in this Perspective.
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