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The Copper Chaperone NosL Forms a Heterometal Site for Cu Delivery to Nitrous Oxide Reductase
Author(s) -
Prasser Benedikt,
Schöner Lisa,
Zhang Lin,
Einsle Oliver
Publication year - 2021
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.202106348
Subject(s) - nitrous oxide reductase , chemistry , chaperone (clinical) , reductase , metal , copper , enzyme , nitrous oxide , active site , bacteria , metal ions in aqueous solution , crystallography , biochemistry , stereochemistry , nitrate reductase , biology , nitrite reductase , genetics , organic chemistry , medicine , pathology
The final step of denitrification is the reduction of nitrous oxide (N 2 O) to N 2 , mediated by Cu‐dependent nitrous oxide reductase (N 2 OR). Its metal centers, Cu A and Cu Z , are assembled through sequential provision of twelve Cu I ions by a metallochaperone that forms part of a nos gene cluster encoding the enzyme and its accessory factors. The chaperone is the nosL gene product, an 18 kDa lipoprotein predicted to reside in the outer membrane of Gram‐negative bacteria. In order to better understand the assembly of N 2 OR, we have produced NosL from Shewanella denitrificans and determined the structure of the metal‐loaded chaperone by X‐ray crystallography. The protein assembled a heterodinuclear metal site consisting of Zn II and Cu I , as evidenced by anomalous X‐ray scattering. While only Cu I is delivered to the enzyme, the stabilizing presence of Zn II is essential for the functionality and structural integrity of the chaperone.