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Your search keyword '"Buren, S [0000-0002-8487-2732]"' showing total 2 results
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2 results on '"Buren, S [0000-0002-8487-2732]"'

1. Environment and coordination of FeMo-co in the nitrogenase metallochaperone NafY

Author

Ministerio de Ciencia, Innovación y Universidades (España), Agencia Estatal de Investigación (España), Payá-Tormo, Lucía [0000-0003-0862-5235], Buren, S [0000-0002-8487-2732], Cuevas-Zuviria, B [0000-0003-1479-9442], Pelton, JG [0000-0002-8627-4445], Wemmer, DE [0000-0001-6252-3390], Rubio, Luis M. [0000-0003-1596-2475], Phillips, Aaron H., Hernandez, Jose A., Payá-Tormo, Lucía, Burén, Stefan, Cuevas-Zuviría, Bruno, Pacios, Luis F., Pelton, J. G., Wemmer, D. E., Rubio, Luis M., Ministerio de Ciencia, Innovación y Universidades (España), Agencia Estatal de Investigación (España), Payá-Tormo, Lucía [0000-0003-0862-5235], Buren, S [0000-0002-8487-2732], Cuevas-Zuviria, B [0000-0003-1479-9442], Pelton, JG [0000-0002-8627-4445], Wemmer, DE [0000-0001-6252-3390], Rubio, Luis M. [0000-0003-1596-2475], Phillips, Aaron H., Hernandez, Jose A., Payá-Tormo, Lucía, Burén, Stefan, Cuevas-Zuviría, Bruno, Pacios, Luis F., Pelton, J. G., Wemmer, D. E., and Rubio, Luis M.

Abstract

In nitrogenase biosynthesis, the iron-molybdenum cofactor (FeMo-co) is externally assembled at scaffold proteins and delivered to the NifDK nitrogenase component by the NafY metallochaperone. Here we have used nuclear magnetic resonance, molecular dynamics, and functional analysis to elucidate the environment and coordination of FeMo-co in NafY. H-121 stands as the key FeMo-co ligand. Regions near FeMo-co diverge from H-121 and include the eta 1, alpha 1, alpha 2 helical lobe and a narrow path between H-121 and C-196.

Published
2021

2. Environment and coordination of FeMo-co in the nitrogenase metallochaperone NafY

Author

Aaron H. Phillips, Luis F. Pacios, Luis M. Rubio, Jose A. Hernandez, Stefan Burén, Jeffrey G. Pelton, David E. Wemmer, Bruno Cuevas-Zuviría, Lucía Payá-Tormo, Ministerio de Ciencia, Innovación y Universidades (España), Agencia Estatal de Investigación (España), Paya-Tormo, L [0000-0003-0862-5235], Buren, S [0000-0002-8487-2732], Cuevas-Zuviria, B [0000-0003-1479-9442], Pelton, JG [0000-0002-8627-4445], Wemmer, DE [0000-0001-6252-3390], Rubio, LM [0000-0003-1596-2475], Paya-Tormo, L, Buren, S, Cuevas-Zuviria, B, Pelton, JG, Wemmer, DE, and Rubio, LM

Subjects
Scaffold protein, biology, Chemistry, Ligand, Protein, Nitrogenase, Binding, Biochemistry, Genetics and Molecular Biology (miscellaneous), Biochemistry, Cofactor, Molecular dynamics, Chemistry (miscellaneous), Metalloproteins, biology.protein, Biophysics, Molecular Biology
Abstract

In nitrogenase biosynthesis, the iron-molybdenum cofactor (FeMo-co) is externally assembled at scaffold proteins and delivered to the NifDK nitrogenase component by the NafY metallochaperone. Here we have used nuclear magnetic resonance, molecular dynamics, and functional analysis to elucidate the environment and coordination of FeMo-co in NafY. H-121 stands as the key FeMo-co ligand. Regions near FeMo-co diverge from H-121 and include the eta 1, alpha 1, alpha 2 helical lobe and a narrow path between H-121 and C-196., Funds for the 900 MHz NMR spectrometer were provided by the NIH through grant GM68933 to D. E. W. This work was also funded by FEDER/Ministerio de Ciencia, Innovación y Universidades-Agencia Estatal de Investigación grant 2017- 88475-R (L. M. R), by Severo Ochoa Program for Centres of Excellence in R&D from Agencia Estatal de Investigación of Spain grant SEV-2016-0672 to the CBGP, and by Midwestern University intramural funds (J. A. H.). L. P.-T. is recipient of FPU16/02284 from Ministerio de Ciencia, Innovaciòn y Universidades

Published
2021

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