Abstract
The final step of denitrification is the reduction of nitrous oxide (N2O) to N2, mediated by Cu‐dependent nitrous oxide reductase (N2OR). Its metal centers, CuA and CuZ, are assembled through sequential provision of twelve CuI 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 N2OR, 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 ZnII and CuI, as evidenced by anomalous X‐ray scattering. While only CuI is delivered to the enzyme, the stabilizing presence of ZnII is essential for the functionality and structural integrity of the chaperone.
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