Investigation of Ca2+-binding sites on the 33 kDa protein in photosystem 2 using as a fluorescence probe

Title:

Investigation of Ca2+-binding sites on the 33 kDa protein in photosystem 2 using as a fluorescence probe

Creator:

Zhang, LiXin, Wang, Jun, and Liang, HouGuo

Identifier:

https://cdk.lib.cas.cz/client/handle/uuid:58412e7d-3842-4edc-a76a-7091b2fc38eb
uuid:58412e7d-3842-4edc-a76a-7091b2fc38eb
urnnbn:urn:nbn:cz:aba007-000fnm

Subject:

aspartic acid, tryptophan, terbium, Spinacia oleracea L., pH titration, non-radiative energy transfer, lanthanides, and glutamic acid

Type:

model:internalpart and TEXT

Format:

print

Description:

Terbium (Tb^'*") was ušed as a fluorescence probe in the study of calcium-binding sites on 33 kDa protein of photosystem 2. The fluorescence of Tb^^ was enhanced markedly when bound to the 33 kDa protein, and the non-radiative energy transfer between tryptophan (Trp) residue and Tb^+, bound to the calcium-binding sites on the 33 kDa protein, took plače. According to the Forster non-radiative energy transfer mechanism, the average distance between the bound Tb3+ and Trp residue was found to be 1.05 nm. The pH titration indicated that major groups in the 33 kDa protein, involved in Ca2+ ions binding, were the carboxylic side groups of the glutamic acid and/or aspartic acid.

Language:

Multiple languages

Rights:

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

Coverage:

203-208 and 45-50

Source:

Photosynthetica | 1995 Volume:31 | Number:2

Harvested from:

CDK

Metadata only:

false