Increasingly precise structural information is available for the FeMo cofactor of nitrogenase. EXAFS spectra of a single crystal of nitrogenase from C. pasteurianum provided MoFe and FeFe distances shorter than those previously determined by X-ray crystallography (2.7 vs. 2.9 Å and 2.61 vs. 2.83 Å, respectively). In addition, a long-range MoFe interaction at 5.1 Å was found. These structural data allow the design of a model of the active center (picture on the right) that is more compact and symmetrical than that based on an X-ray structure analysis having a resolution of 2.2 Å.
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Cramer et al. (1993) studied this question.
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