New light on nitrogenase
Article Abstract:
Five similarities have been identified between the structure of the nitrogenase molybdenum-iron protein of Azotobacter vinelandii and the structure of the photosynthetic reaction center of the purple bacterium Rhodopseudomonas viridis. Both have unidirectional electron transfers, two types of subunit, separate transfer pathways for protons and electrons, buried reducible substrate site and inefficient energy coupling in ATP hydrolysis and light harvesting. This study by Jongsun Kim and D.C. Rees indicates a role for nitrogenase beyond nitrogen fixation.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1992
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Structure of ADP.A1F4-stabilized nitrogenase complex and its implications for signal transduction
Article Abstract:
A detailed structural analysis of the enzyme nitrogenase, which is made up of Fe-protein and MoFe-protein, can provide valuable information about how signal transduction occurs in multiprotein complexes. Recent research has focused on determining the structure of the -360K multiprotein nitrogenase complex stabilized with ADP.A1F4. It was found that the Fe-protein experiences significant conformational changes. Interactions at the interface between the Fe-protein subunits are responsible for stabilizing the beta-phosphate and A1F4 groups.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1997
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Crystallographic structure and functional implications of the nitrogenase molybdenum-iron protein from Azobacter vinelandii
Article Abstract:
The crystalline form of the bacterium Azotobacter vinelandii's nitrogenase molybdenum-iron protein has been ascertained at the 2.7 angstrom level. The form consists of an alpha-2-beta-2 tetrameter whose alpha- and beta-subunits contain similar polypeptide folds. Although the alpha-subunit entirely encloses the FeMo-cofactor, the subunits' interface houses the P-cluster pair. Nitrogenase and other electron transfer systems resemble each other structurally.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1992
User Contributions:
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