Redox activated proton transfer through a redundant network in the Qo site of Cytochrome bc1 (2025)
- Autor:
- Autor USP: ARANTES, GUILHERME MENEGON - IQ
- Unidade: IQ
- DOI: 10.1021/acs.jcim.4c02361
- Subjects: MECÂNICA QUÂNTICA; OXIDAÇÃO; REDUÇÃO
- Agências de fomento:
- Language: Inglês
- Imprenta:
- Publisher place: Washington
- Date published: 2025
- Source:
- Título: Journal of Chemical Information and Modeling
- ISSN: 1549-9596
- Volume/Número/Paginação/Ano: v. 65, n. 5, p. 2660−2669, 2025
- Este periódico é de assinatura
- Este artigo é de acesso aberto
- URL de acesso aberto
- Cor do Acesso Aberto: hybrid
- Licença: cc-by
-
ABNT
ARANTES, Guilherme Menegon. Redox activated proton transfer through a redundant network in the Qo site of Cytochrome bc1. Journal of Chemical Information and Modeling, v. 65, n. 5, p. 2660−2669, 2025Tradução . . Disponível em: https://dx.doi.org/10.1021/acs.jcim.4c02361. Acesso em: 26 dez. 2025. -
APA
Arantes, G. M. (2025). Redox activated proton transfer through a redundant network in the Qo site of Cytochrome bc1. Journal of Chemical Information and Modeling, 65( 5), 2660−2669. doi:10.1021/acs.jcim.4c02361 -
NLM
Arantes GM. Redox activated proton transfer through a redundant network in the Qo site of Cytochrome bc1 [Internet]. Journal of Chemical Information and Modeling. 2025 ; 65( 5): 2660−2669.[citado 2025 dez. 26 ] Available from: https://dx.doi.org/10.1021/acs.jcim.4c02361 -
Vancouver
Arantes GM. Redox activated proton transfer through a redundant network in the Qo site of Cytochrome bc1 [Internet]. Journal of Chemical Information and Modeling. 2025 ; 65( 5): 2660−2669.[citado 2025 dez. 26 ] Available from: https://dx.doi.org/10.1021/acs.jcim.4c02361 - Computational molecular bioenergetics: simulations of iron-sulfur proteins and mobile natural quinones
- Computational method to cluster complexes of small ligands and flexible proteins
- Mechanism of bond dissociation in metalloproteins under stress
- Effects of lipid composition on membrane distribution and permeability of natural quinones
- Force-induced chemical reactions on the metal centre in a single metalloprotein molecule
- Parametrization of an ubiquinone force field and simulation of membrane partition, diffusion and redox potentials
- Ligand receptor affinities computed by an adapted linear interaction model for continuum electrostatics and by protein conformational averaging
- Theoretical modeling of low-energy electronic absorption bands in reduced cobaloximes
- Homolytic cleavage of `FE´-`S´ bonds in rubredoxin under mechanical stress
- Fe-S bond stability in simple models and in mechanically stretched rubredoxin
Informações sobre o DOI: 10.1021/acs.jcim.4c02361 (Fonte: oaDOI API)
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