Structures of substrate- and product-bound forms of a multi-domain copper nitrite reductase shed light on the role of domain tethering in protein complexes (2020)
- Authors:
- Autor USP: GARRATT, RICHARD CHARLES - IFSC
- Unidade: IFSC
- DOI: 10.1107/S2052252520005230
- Subjects: NITROGÊNIO; DESNITRIFICAÇÃO; CATÁLISE
- Keywords: Nitrogen cycle; Denitrification; Copper-containing nitrite reductase; Electron transfer; Catalysis; Structural biology
- Agências de fomento:
- Language: Inglês
- Imprenta:
- Source:
- Este periódico é de acesso aberto
- Este artigo NÃO é de acesso aberto
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ABNT
SASAKI, Daisuke et al. Structures of substrate- and product-bound forms of a multi-domain copper nitrite reductase shed light on the role of domain tethering in protein complexes. IUCrJ, v. 7, p. 557-565 + sup1-sup6, 2020Tradução . . Disponível em: https://doi.org/10.1107/S2052252520005230. Acesso em: 24 fev. 2026. -
APA
Sasaki, D., Watanabe, T. F., Eady, R. R., Garratt, R. C., Antonyuk, S. V., & Hasnain, S. S. (2020). Structures of substrate- and product-bound forms of a multi-domain copper nitrite reductase shed light on the role of domain tethering in protein complexes. IUCrJ, 7, 557-565 + sup1-sup6. doi:10.1107/S2052252520005230 -
NLM
Sasaki D, Watanabe TF, Eady RR, Garratt RC, Antonyuk SV, Hasnain SS. Structures of substrate- and product-bound forms of a multi-domain copper nitrite reductase shed light on the role of domain tethering in protein complexes [Internet]. IUCrJ. 2020 ; 7 557-565 + sup1-sup6.[citado 2026 fev. 24 ] Available from: https://doi.org/10.1107/S2052252520005230 -
Vancouver
Sasaki D, Watanabe TF, Eady RR, Garratt RC, Antonyuk SV, Hasnain SS. Structures of substrate- and product-bound forms of a multi-domain copper nitrite reductase shed light on the role of domain tethering in protein complexes [Internet]. IUCrJ. 2020 ; 7 557-565 + sup1-sup6.[citado 2026 fev. 24 ] Available from: https://doi.org/10.1107/S2052252520005230 - Estructura de la fosfofructoquinasa-2 de Escherichia coli presencia del motivo conservado NXXE en el sitio activo
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Informações sobre o DOI: 10.1107/S2052252520005230 (Fonte: oaDOI API)
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