Structure of a Cofactor-Deficient Nitrogenase MoFe Protein

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Science  12 Apr 2002:
Vol. 296, Issue 5566, pp. 352-356
DOI: 10.1126/science.1070010

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One of the most complex biosynthetic processes in metallobiochemistry is the assembly of nitrogenase, the key enzyme in biological nitrogen fixation. We describe here the crystal structure of an iron-molybdenum cofactor–deficient form of the nitrogenase MoFe protein, into which the cofactor is inserted in the final step of MoFe protein assembly. The MoFe protein folds as a heterotetramer containing two copies each of the homologous α and β subunits. In this structure, one of the three α subunit domains exhibits a substantially changed conformation, whereas the rest of the protein remains essentially unchanged. A predominantly positively charged funnel is revealed; this funnel is of sufficient size to accommodate insertion of the negatively charged cofactor.

  • * These authors contributed equally to this work.

  • To whom correspondence should be addressed. E-mail: dcrees{at}

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