The copper chaperone NosL forms a heterometal site for Cu delivery to nitrous oxide reductase
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
- Standort
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Deutsche Nationalbibliothek Frankfurt am Main
- Umfang
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Online-Ressource
- Sprache
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Englisch
- Anmerkungen
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Angewandte Chemie. International Edition. - 60, 34 (2021) , 18810-18814, ISSN: 1521-3773
- Ereignis
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Veröffentlichung
- (wo)
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Freiburg
- (wer)
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Universität
- (wann)
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2021
- Urheber
- DOI
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10.1002/anie.202106348
- URN
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urn:nbn:de:bsz:25-freidok-2200103
- Rechteinformation
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Kein Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
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25.03.2025, 13:41 MEZ
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Beteiligte
- Prasser, Benedikt
- Schöner, Lisa
- Zhang, Lin
- Einsle, Oliver
- Universität
Entstanden
- 2021
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