Apoprotein heterogeneity increases spectral disorder and a step-wise modification of the B850 fluorescence peak position.
Biochim Biophys Acta Bioenerg
; 1859(2): 137-144, 2018 Feb.
Article
en En
| MEDLINE
| ID: mdl-29174011
ABSTRACT
It has already been established that the quaternary structure of the main light-harvesting complex (LH2) from the photosynthetic bacterium Rhodopseudomonas palustris is a nonameric 'ring' of PucAB heterodimers and under low-light culturing conditions an increased diversity of PucB synthesis occurs. In this work, single molecule fluorescence emission studies show that different classes of LH2 'rings' are present in "low-light" adapted cells and that an unknown chaperon process creates multiple sub-types of 'rings' with more conformational sub-states and configurations. This increase in spectral disorder significantly augments the cross-section for photon absorption and subsequent energy flow to the reaction centre trap when photon availability is a limiting factor. This work highlights yet another variant used by phototrophs to gather energy for cellular development.
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Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Apoproteínas
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Rhodopseudomonas
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Proteínas Bacterianas
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Complejos de Proteína Captadores de Luz
Idioma:
En
Año:
2018
Tipo del documento:
Article