Electron microscopy of the Mo‐Fe‐protein from Azotobacter vinelandii nitrogenase

V. L. TSUPRUN; I. Z. MITSOVA; I. S. BLAZHCHUK; R. I. GVOZDEV; E. V. ORLOVA; N. A. KISELEV

doi:10.1111/j.1432-1033.1985.tb08937.x

Electron microscopy of the Mo‐Fe‐protein from Azotobacter vinelandii nitrogenase

V. L. TSUPRUN, I. Z. MITSOVA, I. S. BLAZHCHUK, R. I. GVOZDEV, E. V. ORLOVA, N. A. KISELEV

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Abstract

The quaternary structure of the Mo‐Fe‐protein from Azotobacter vinelandii has been studied by electron microscopy. A model of the molecule of the Mo‐Fe‐protein has been proposed: two α subunits are displaced relative to two β subunits along a twofold axis, so the molecule can be characterized by the point‐group pseudosymmetry 222. Computer averaging of the images showed that one of the projections of the molecule could be characterized by twofold rotational symmetry. Micrographs of nitrogenase recombined complex (Mo‐Fe‐protein + Fe‐protein) have been obtained. They showed particles close in size and form to the Mo‐Fe‐protein molecule. Therefore, it has been proposed that the Fe‐protein could be situated in the central cavity of Mo‐Fe‐protein.

Original language	English (US)
Pages (from-to)	389-392
Number of pages	4
Journal	European Journal of Biochemistry
Volume	149
Issue number	2
DOIs	https://doi.org/10.1111/j.1432-1033.1985.tb08937.x
State	Published - Jun 1985

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title = "Electron microscopy of the Mo‐Fe‐protein from Azotobacter vinelandii nitrogenase",

abstract = "The quaternary structure of the Mo‐Fe‐protein from Azotobacter vinelandii has been studied by electron microscopy. A model of the molecule of the Mo‐Fe‐protein has been proposed: two α subunits are displaced relative to two β subunits along a twofold axis, so the molecule can be characterized by the point‐group pseudosymmetry 222. Computer averaging of the images showed that one of the projections of the molecule could be characterized by twofold rotational symmetry. Micrographs of nitrogenase recombined complex (Mo‐Fe‐protein + Fe‐protein) have been obtained. They showed particles close in size and form to the Mo‐Fe‐protein molecule. Therefore, it has been proposed that the Fe‐protein could be situated in the central cavity of Mo‐Fe‐protein.",

author = "TSUPRUN, {V. L.} and MITSOVA, {I. Z.} and BLAZHCHUK, {I. S.} and GVOZDEV, {R. I.} and ORLOVA, {E. V.} and KISELEV, {N. A.}",

year = "1985",

month = jun,

doi = "10.1111/j.1432-1033.1985.tb08937.x",

language = "English (US)",

volume = "149",

pages = "389--392",

journal = "European Journal of Biochemistry",

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TY - JOUR

T1 - Electron microscopy of the Mo‐Fe‐protein from Azotobacter vinelandii nitrogenase

AU - TSUPRUN, V. L.

AU - MITSOVA, I. Z.

AU - BLAZHCHUK, I. S.

AU - GVOZDEV, R. I.

AU - ORLOVA, E. V.

AU - KISELEV, N. A.

PY - 1985/6

Y1 - 1985/6

N2 - The quaternary structure of the Mo‐Fe‐protein from Azotobacter vinelandii has been studied by electron microscopy. A model of the molecule of the Mo‐Fe‐protein has been proposed: two α subunits are displaced relative to two β subunits along a twofold axis, so the molecule can be characterized by the point‐group pseudosymmetry 222. Computer averaging of the images showed that one of the projections of the molecule could be characterized by twofold rotational symmetry. Micrographs of nitrogenase recombined complex (Mo‐Fe‐protein + Fe‐protein) have been obtained. They showed particles close in size and form to the Mo‐Fe‐protein molecule. Therefore, it has been proposed that the Fe‐protein could be situated in the central cavity of Mo‐Fe‐protein.

AB - The quaternary structure of the Mo‐Fe‐protein from Azotobacter vinelandii has been studied by electron microscopy. A model of the molecule of the Mo‐Fe‐protein has been proposed: two α subunits are displaced relative to two β subunits along a twofold axis, so the molecule can be characterized by the point‐group pseudosymmetry 222. Computer averaging of the images showed that one of the projections of the molecule could be characterized by twofold rotational symmetry. Micrographs of nitrogenase recombined complex (Mo‐Fe‐protein + Fe‐protein) have been obtained. They showed particles close in size and form to the Mo‐Fe‐protein molecule. Therefore, it has been proposed that the Fe‐protein could be situated in the central cavity of Mo‐Fe‐protein.

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JO - European Journal of Biochemistry

JF - European Journal of Biochemistry

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ER -

Electron microscopy of the Mo‐Fe‐protein from Azotobacter vinelandii nitrogenase

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