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

doi:10.1016/0162-0134(86)80015-0

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

Otolaryngology

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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 language	English (US)
Pages (from-to)	141-146
Number of pages	6
Journal	Journal of Inorganic Biochemistry
Volume	27
Issue number	2
DOIs	https://doi.org/10.1016/0162-0134(86)80015-0
State	Published - Jun 1986

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title = "Electron microscopy of the nitrogenase molecule from azotobacter vinelandii",

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.",

author = "Tsuprun, {V. L.} and Orlova, {E. V.} and Kiselev, {N. A.} and Mitsova, {I. Z.} and Blazshchuk, {I. S.} and Gvozdev, {R. I.}",

year = "1986",

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doi = "10.1016/0162-0134(86)80015-0",

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T1 - Electron microscopy of the nitrogenase molecule from azotobacter vinelandii

AU - Tsuprun, V. L.

AU - Orlova, E. V.

AU - Kiselev, N. A.

AU - Mitsova, I. Z.

AU - Blazshchuk, I. S.

AU - Gvozdev, R. I.

PY - 1986/6

Y1 - 1986/6

N2 - 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.

AB - 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.

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JO - Journal of Inorganic Biochemistry

JF - Journal of Inorganic Biochemistry

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ER -

Electron microscopy of the nitrogenase molecule from azotobacter vinelandii

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