Three-Dimensional Structure of Cytochrome c Nitrite Reductase As Determined by Cryo-Electron Microscopy

The structure of cytochrome c nitrite reductase from the bacterium Thioalkalivibrio nitratireducens was determined by cryo-electron microscopy (cryo-EM) at a 2.56 Å resolution. Possible structural heterogeneity of the enzyme was assessed. The backbone and side-chain orientations in the cryo-EM-based...

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Detalles Bibliográficos
Autores principales: Baymukhametov, T. N., Chesnokov, Y. M., Pichkur, E. B., Boyko, K. M., Tikhonova, T. V., Myasnikov, A. G., Vasiliev, A. L., Lipkin, A. V., Popov, V. O., Kovalchuk, M. V.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: A.I. Gordeyev 2018
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6209398/
https://www.ncbi.nlm.nih.gov/pubmed/30397526
Descripción
Sumario:The structure of cytochrome c nitrite reductase from the bacterium Thioalkalivibrio nitratireducens was determined by cryo-electron microscopy (cryo-EM) at a 2.56 Å resolution. Possible structural heterogeneity of the enzyme was assessed. The backbone and side-chain orientations in the cryo-EM-based model are, in general, similar to those in the high-resolution X-ray diffraction structure of this enzyme.

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