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Looking at Nitrogenase: Insights from Modern Structural Approaches

Wenke, Belinda B. and Spatzal, Thomas (2018) Looking at Nitrogenase: Insights from Modern Structural Approaches. In: Metallocofactors that Activate Small Molecules: With Focus on Bioinorganic Chemistry. Structure and Bonding. No.179. Springer , Cham, pp. 1-13. ISBN 978-3-030-25896-2.

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Nitrogenase, the primary biological source of fixed nitrogen, has been studied by various biochemical and biophysical methods to determine the mechanism of nitrogen reduction to ammonia. Previously, structural studies have contributed to determining the arrangement and identity of the unique metallocofactors of the as-isolated nitrogenase enzyme. Due to the multi-protein, dynamic nature of catalysis in nitrogenase, structurally capturing intermediates is not trivial. Recently, we have developed methods for preparing crystallographic samples of nitrogenase from active assay mixtures. The “out-of-assay” approach has yielded structures of small molecules bound to the active site cofactor, revealing an unexpected rearrangement of the belt sulfur atoms. The activity-based methods provide a framework for accessing non-resting states of the cofactor and introduce new questions surrounding the controlled binding and release of substrates. In the following, we discuss recent structural advances in the field and the novel directions for future activity-based research.

Item Type:Book Section
Related URLs:
URLURL TypeDescription
Wenke, Belinda B.0000-0003-3214-6197
Spatzal, Thomas0000-0002-9136-5915
Additional Information:© 2018 Springer Nature Switzerland AG. First Online: 09 November 2018. The authors thank Douglas C. Rees, James B. Howard and Kathryn A. Perez for their support and helpful discussions, as well as the scientists of Beamline 12-2, Stanford Synchrotron Radiation Lightsource (Department of Energy, DE-AC02-76SF00515). The authors are supported by the National Institute of Health grant GM45162 as well as NIH/NRSA training grant 5 T32 GM07616.
Funding AgencyGrant Number
Department of Energy (DOE)DE-AC02-76SF00515
NIH Predoctoral Fellowship5 T32 GM07616
Subject Keywords:CO; FeMo-cofactor; Freeze quench; Nitrogenase; Selenium; X-ray crystallography
Series Name:Structure and Bonding
Issue or Number:179
Record Number:CaltechAUTHORS:20191220-103957225
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Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:100393
Deposited By: Tony Diaz
Deposited On:21 Dec 2019 16:55
Last Modified:16 Nov 2021 17:53

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