Electron microscopy of the nitrogenase molecule from azotobacter vinelandii

V. L. Tsuprun, E. V. Orlova, N. A. Kiselev, I. Z. Mitsova, I. S. Blazshchuk, R. I. Gvozdev

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2 Scopus citations

Abstract

The quaternary structure of nitrogenase recombined complex (Mo-Fe protein + Fe protein) from Azotobacter vinelandii has been studied by electron microscopy for comparison with the structure of the Mo-Fe protein proposed earlier. Computer averaging of the images showed that one of the projections of the Mo-Fe protein could be characterized by twofold rotational symmetry and the molecule itself has 222 pseudosymmetry. Nitrogenase recombined complex in the same projection revealed additional protein densities that are associated with the Fe protein. It has been suggested that the Fe protein dimer in nitrogenase complex is located in cavities of the central part of the Mo-Fe protein.

Original languageEnglish (US)
Pages (from-to)141-146
Number of pages6
JournalJournal of Inorganic Biochemistry
Volume27
Issue number2
DOIs
StatePublished - Jun 1986

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Copyright 2014 Elsevier B.V., All rights reserved.

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