Structure of a Cofactor-Deficient Nitrogenase MoFe Protein
2002; American Association for the Advancement of Science; Volume: 296; Issue: 5566 Linguagem: Inglês
10.1126/science.1070010
ISSN1095-9203
AutoresBenedikt Schmid, Markus W. Ribbe, Oliver Einsle, Mika Yoshida, Leonard M. Thomas, Dennis R. Dean, Douglas C. Rees, Barbara K. Burgess,
Tópico(s)Hydrogen Storage and Materials
ResumoOne 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.
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