1. Structural Characterization of Poised States in the Oxygen Sensitive Hydrogenases and Nitrogenases.
- Author
-
Artz JH, Zadvornyy OA, Mulder DW, King PW, and Peters JW
- Subjects
- Ammonia metabolism, Archaea enzymology, Bacteria enzymology, Bacterial Proteins chemistry, Bacterial Proteins metabolism, Biocatalysis, Catalytic Domain, Cryoelectron Microscopy, Crystallization, Crystallography, Hydrogen metabolism, Hydrogenase metabolism, Iron metabolism, Molecular Conformation, Nitrogen metabolism, Nitrogenase metabolism, Protein Conformation, Protons, Structure-Activity Relationship, Hydrogenase chemistry, Nitrogenase chemistry, Oxygen metabolism
- Abstract
The crystallization of FeS cluster-containing proteins has been challenging due to their oxygen sensitivity, and yet these enzymes are involved in many critical catalytic reactions. The last few years have seen a wealth of innovative experiments designed to elucidate not just structural but mechanistic insights into FeS cluster enzymes. Here, we focus on the crystallization of hydrogenases, which catalyze the reversible reduction of protons to hydrogen, and nitrogenases, which reduce dinitrogen to ammonia. A specific focus is given to the different experimental parameters and strategies that are used to trap distinct enzyme states, specifically, oxidants, reductants, and gas treatments. Other themes presented here include the recent use of Cryo-EM, and how coupling various spectroscopies to crystallization is opening up new approaches for structural and mechanistic analysis., (© 2017 Elsevier Inc. All rights reserved.)
- Published
- 2017
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