Ca2+ stabilization of respiratory complex I from Escherichia coli.
FEMS Microbiol Lett
; 365(12)2018 06 01.
Article
en En
| MEDLINE
| ID: mdl-29668960
ABSTRACT
Stability of the membrane-bound and purified H+-translocating NADHubiquinone oxidoreductase, Complex I, was studied. The loss of the enzyme activity is strongly increased by alkaline pH and dilution of the sample. Complex I inactivation is prevented specifically by a low concentration of Ca2+ and/or an intracellular stabilization factor (ISF). The action of both, Ca2+ and ISF, on Complex I stability is interdependent. The data are discussed in terms of a release of structural Ca2+ as a reason for Complex I decay and an effect of ISF on the affinity and/or accessibility of Ca2+-binding site.
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Calcio
/
Complejo I de Transporte de Electrón
/
Escherichia coli
Idioma:
En
Revista:
FEMS Microbiol Lett
Año:
2018
Tipo del documento:
Article
País de afiliación:
Finlandia