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

Research output: Contribution to journal › Article › peer-review

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 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

Bibliographical note

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

Publisher link

10.1016/0162-0134(86)80015-0

Find It

Find It at U of M Libraries

Cite this

@article{0bb4be4bff214047aa8c45f12a88a841,

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",

month = jun,

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

language = "English (US)",

volume = "27",

pages = "141--146",

journal = "Journal of Inorganic Biochemistry",

issn = "0162-0134",

publisher = "Elsevier Inc.",

number = "2",

}

TY - JOUR

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.

UR - http://www.scopus.com/inward/record.url?scp=46149133588&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=46149133588&partnerID=8YFLogxK

U2 - 10.1016/0162-0134(86)80015-0

DO - 10.1016/0162-0134(86)80015-0

M3 - Article

AN - SCOPUS:46149133588

VL - 27

SP - 141

EP - 146

JO - Journal of Inorganic Biochemistry

JF - Journal of Inorganic Biochemistry

SN - 0162-0134

IS - 2

ER -

Electron microscopy of the nitrogenase molecule from azotobacter vinelandii

Abstract

Bibliographical note

Publisher link

Find It

Other files and links

Fingerprint

Cite this