How inter-subunit contacts in the membrane domain of complex I affect proton transfer energetics.
Biochim Biophys Acta Bioenerg
; 1859(9): 734-741, 2018 09.
Article
en En
| MEDLINE
| ID: mdl-29883589
ABSTRACT
The respiratory complex I is a redox-driven proton pump that employs the free energy released from quinone reduction to pump protons across its complete ca. 200â¯Å wide membrane domain. Despite recently resolved structures and molecular simulations, the exact mechanism for the proton transport process remains unclear. Here we combine large-scale molecular simulations with quantum chemical density functional theory (DFT) models to study how contacts between neighboring antiporter-like subunits in the membrane domain of complex I affect the proton transfer energetics. Our combined results suggest that opening of conserved Lys/Glu ion pairs within each antiporter-like subunit modulates the barrier for the lateral proton transfer reactions. Our work provides a mechanistic suggestion for key coupling effects in the long-range force propagation process of complex I.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Protones
/
Membrana Celular
/
Thermus thermophilus
/
Complejo I de Transporte de Electrón
/
Metabolismo Energético
Idioma:
En
Revista:
Biochim Biophys Acta Bioenerg
Año:
2018
Tipo del documento:
Article
País de afiliación:
Alemania