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HERO ID
7824589
Reference Type
Journal Article
Title
DETERMINATION OF THE MOLECULAR-SIZE OF THE BINDING-SITE FOR THE MANGANESE-STABILIZING 33-KDA PROTEIN IN PHOTOSYSTEM-II MEMBRANES
Author(s)
Takahashi, M; Asada, K
Year
1991
Is Peer Reviewed?
1
Journal
Biochimica et Biophysica Acta
ISSN:
0006-3002
EISSN:
1878-2434
Publisher
ELSEVIER SCIENCE BV
Location
AMSTERDAM
Volume
1059
Issue
3
Page Numbers
361-364
DOI
10.1016/S0005-2728(05)80222-1
Web of Science Id
WOS:A1991GG96800013
URL
https://linkinghub.elsevier.com/retrieve/pii/S0005272805802221
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Abstract
A radiation-inactivation study revealed that the manganese-stabilizing 33 kDa protein (MSP) binds to a site of only 13 kDa in CaCl2-treated Photosystem (PS) II complexes. From the coincidence of this size with molecular weight it appears that a cytochrome b-559 heterodimer is responsible for the functional binding of MSP to the PS II reaction center.
Keywords
CYTOCHROME B-559; MANGANESE-STABILIZING 33-KDA PROTEIN; OXYGEN EVOLUTION; PHOTOSYSTEM-II; RADIATION INACTIVATION; (SPINACH)
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