Structural characteristics of extra-membrane domains and guanidine hydrochloride-induced denaturation of photosystem 2 core antenna complexes CP43 and CP47

Title:

Structural characteristics of extra-membrane domains and guanidine hydrochloride-induced denaturation of photosystem 2 core antenna complexes CP43 and CP47

Creator:

Qu, Y.-G., Gong, Y.-D., Guo, S.-K., Li, L.-B., and Kuang, T.-Y.

Identifier:

https://cdk.lib.cas.cz/client/handle/uuid:8b9e03b0-16b7-4941-b479-8a107847a2b2
uuid:8b9e03b0-16b7-4941-b479-8a107847a2b2
issn:0300-3604
doi:10.1007/s11099-006-0049-y

Subject:

aromatic amino acid, chlorophyll, circular dichronism, CP43, CP47, denaturation, energy transfer, extramembrane domain, fluorescence, guanidine hydrochloride, and β-carotene

Type:

model:article and TEXT

Format:

bez média and svazek

Description:

The structural characteristics of the extra-membrane domains and guanidine hydrochloride-induced denaturation of photosystem 2 (PS2) core antenna complexes CP43 and CP47 were investigated using fluorescence emission and circular dichroism (CD) spectra. The extra-membrane domains of CP43 and CP47 possessed a certain degree of secondary and tertiary structure and not a complete random coil conformation. The tertiary structure and the chlorophyll (Chl) a microenvironment of CP47 were more sensitive to guanidine hydrochloride (GuHCl) than that of CP43. Changes in energy transfer from β-carotene to Chl a corresponded well to changes in the tertiary structure while their correlation with changes in the secondary structure was rather poor. Unlike most of water-soluble proteins, both CP43 and CP47 are partly resistant to denaturation induced by guanidine hydrochloride (GuHCl); the denaturation of CP43 or CP47 is not a two-state process. Those features most probably reflect their character as intrinsic membrane proteins. and Y.-G. Qu ... [et al.].

Language:

Multiple languages

Rights:

http://creativecommons.org/licenses/by-nc-sa/4.0/
policy:public

Coverage:

447-453

Source:

Photosynthetica | 2006 Volume:44 | Number:3

Harvested from:

CDK

Metadata only:

false