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Crystallization of Nitrogenase Proteins

Wenke, Belinda B. and Arias, Renee J. and Spatzal, Thomas (2018) Crystallization of Nitrogenase Proteins. In: Metalloproteins. Methods in Molecular Biology. No.1876. Humana Press , New York, NY, pp. 155-165. ISBN 978-1-4939-8863-1. https://resolver.caltech.edu/CaltechAUTHORS:20181022-102730676

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Abstract

Nitrogenase is the only known enzymatic system capable of reducing atmospheric dinitrogen to ammonia. This unique reaction requires tightly choreographed interactions between the nitrogenase component proteins, the molybdenum–iron (MoFe)- and iron (Fe)-proteins, as well as regulation of electron transfer between multiple metal centers that are only found in these components. Several decades of research beginning in the 1950s yielded substantial information of how nitrogenase manages the task of N2 fixation. However, key mechanistic steps in this highly oxygen-sensitive and ATP-intensive reaction have only recently been identified at an atomic level. A critical part in any mechanistic elucidation is the necessity to connect spectroscopic and functional properties of the component proteins to the detailed three-dimensional structures. Structural information derived from X-ray diffraction (XRD) methods has provided detailed atomic insights into the enzyme system and, in particular, its active site FeMo-cofactor. The following chapter outlines the general protocols for the crystallization of Azotobacter vinelandii (Av) nitrogenase component proteins, with a special emphasis on different applications, such as high-resolution XRD, single-crystal spectroscopy, and the structural characterization of bound inhibitors.


Item Type:Book Section
Related URLs:
URLURL TypeDescription
https://doi.org/10.1007/978-1-4939-8864-8_10DOIArticle
ORCID:
AuthorORCID
Wenke, Belinda B.0000-0003-3214-6197
Arias, Renee J.0000-0002-6505-7513
Spatzal, Thomas0000-0002-9136-5915
Additional Information:© 2019 Springer Science+Business Media, LLC, part of Springer Nature.
Series Name:Methods in Molecular Biology
Issue or Number:1876
Record Number:CaltechAUTHORS:20181022-102730676
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20181022-102730676
Official Citation:q
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:90320
Collection:CaltechAUTHORS
Deposited By: Tony Diaz
Deposited On:22 Oct 2018 21:16
Last Modified:14 Oct 2019 18:24

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