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Science 12 April 2002:
Vol. 296. no. 5566, pp. 352 - 356
DOI: 10.1126/science.1070010
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Reports

Structure of a Cofactor-Deficient Nitrogenase MoFe Protein

Benedikt Schmid,1* Markus W. Ribbe,4* Oliver Einsle,13 Mika Yoshida,13 Leonard M. Thomas,23 Dennis R. Dean,5 Douglas C. Rees,13dagger Barbara K. Burgess4

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 alpha  and beta  subunits. In this structure, one of the three alpha  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.

1 Division of Chemistry and Chemical Engineering, Mail Code 147-75CH;
2 Division of Biology, Mail Code 156-29;
3 Howard Hughes Medical Institute, California Institute of Technology, Pasadena, CA 91125, USA.
4 Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697-3900, USA.
5 Department of Biochemistry, Virginia Polytechnic Institute and State University, Blacksburg, VA 24061, USA.
*   These authors contributed equally to this work.

dagger    To whom correspondence should be addressed. E-mail: dcrees{at}caltech.edu

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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
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Comparison of Iron-Molybdenum Cofactor-deficient Nitrogenase MoFe Proteins by X-ray Absorption Spectroscopy: IMPLICATIONS FOR P-CLUSTER BIOSYNTHESIS.
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