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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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Abstract

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}caltech.edu

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