Crystallographic structure and functional implications of the nitrogenase molybdenum-iron protein from Azotobacter vinelandii

The crystal structure of the nitrogenase molybdenum-iron protein from Azotobacter vinelandii has been determined at 2.7 angstrom resolution. The alpha- and beta-subunits in this alpha 2 beta 2 tetramer have similar polypeptide folds. The FeMo-cofactor is completely encompassed by the alpha-subunit,...

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Bibliographic Details
Published inNature (London) Vol. 360; no. 6404; pp. 553 - 560
Main Authors Kim, J, Rees, D.C
Format Journal Article
LanguageEnglish
Published London Nature Publishing 10.12.1992
Nature Publishing Group
Subjects
Atoms & subatomic particles
Azotobacter vinelandii
Bacteriology
Biological and medical sciences
electron transfer
Fundamental and applied biological sciences. Psychology
iron
Metabolism. Enzymes
Microbiology
Molybdenum
molybdenum-iron protein
nitrogen fixation
nitrogenase
Proteins
structure
X-ray crystallography
Enzymatic activity
Azotobacteraceae
Enzyme
Reaction center
Nitrogenase
Bacteria
Azotobacter vinelandii
Crystalline structure
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Summary:The crystal structure of the nitrogenase molybdenum-iron protein from Azotobacter vinelandii has been determined at 2.7 angstrom resolution. The alpha- and beta-subunits in this alpha 2 beta 2 tetramer have similar polypeptide folds. The FeMo-cofactor is completely encompassed by the alpha-subunit, whereas the P-cluster pair occurs at the interface between alpha- and beta-subunits. Structural similarities are apparent between nitrogenase and other electron transfer systems, including hydrogenases and the photosynthetic reaction centre.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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ISSN:0028-0836
1476-4687
DOI:10.1038/360553a0