Role of Calcium in Secondary Structure Stabilization during Maturation of Nitrous Oxide Reductase.

Biochemistry
Lisa Schneider, Oliver Einsle

Abstract

The copper enzyme nitrous oxide reductase catalyzes the two-electron reduction of nitrous oxide N₂O to dinitrogen N₂. Its maturation largely occurs in the periplasm and includes the insertion of at least one Ca²⁺ ion per monomer. Here we have investigated the role of this structural cation in recombinantly produced apo-N₂OR from Shewanella denitrificans and have determined the three-dimensional structure of the protein by X-ray crystallography. In the absence of Ca²⁺, substantial parts of the enzyme surrounding the binding sites for the copper ions show structural disorder. Reconstitution of the binuclear CuA site was possible in vitro but required the presence of Ca²⁺ ions for a stable insertion of the center. In contrast, an excess of Ca²⁺ prevented copper insertion, and the structural analysis of the Ca²⁺apo form revealed that the cation is sufficient to structure the disordered regions of the protein even in the absence of Cu ions, indicating that the geometry of the two noncanonical copper centers is largely predetermined by the protein structure.

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Citations

Mar 16, 2017·Acta Crystallographica. Section D, Structural Biology·Heping ZhengWladek Minor
Jun 14, 2019·Proceedings of the National Academy of Sciences of the United States of America·Lin ZhangOliver Einsle
Dec 30, 2020·International Journal of Molecular Sciences·Velky AhumadaLuis Caraballo
Feb 29, 2020·Chemical Reviews·Christina FerousiKyle M Lancaster
Mar 12, 2021·Coordination Chemistry Reviews·Suresh C Rathnayaka, Neal P Mankad
Mar 5, 2019·Food Chemistry·Marcelo D PolêtoAntonio Fernandes De Carvalho
Dec 31, 2020·Journal of the American Chemical Society·Lin ZhangOliver Einsle
Sep 21, 2017·Journal of Inorganic Biochemistry·Cíntia CarreiraIsabel Moura

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