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Cited by 186

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Structure of a Cofactor-Deficient Nitrogenase MoFe Protein

Schmid, Benedikt, Ribbe, Markus W., Einsle, Oliver, Yoshida, Mika, Thomas, Leonard M., Dean, Dennis R., Rees, Douglas C., Burgess, Barbara K.·2002·Science

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.

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Metadata

Authors
Schmid, B., Ribbe, M. W., Einsle, O., Yoshida, M., Thomas, L. M., Dean, D. R., Rees, D. C., & Burgess, B. K.
Venue
Science
Published
2002-04-12
Volume
296
Issue
5566
Pages
352-356
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2023278164
Cited by
186
References
2
FWCI
12.94
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Structure of a Cofactor-Deficient Nitrogenase MoFe Protein. https://app.cochat.ai/papers/10.1126/science.1070010
The paper
Schmid, B., Ribbe, M. W., Einsle, O., Yoshida, M., Thomas, L. M., Dean, D. R., Rees, D. C., & Burgess, B. K. (2002). Structure of a Cofactor-Deficient Nitrogenase MoFe Protein. Science. https://doi.org/10.1126/science.1070010

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.