Abstract:
:PsbU is one of the extrinsic proteins in red algal Photosystem II (PSII) and functions to optimize the availability of Ca(2+) and Cl(-) cofactors for water oxidation. To determine the functional residue of PsbU, we constructed various PsbU mutants from a red alga Cyanidium caldarium and reconstituted these mutants with the red algal PSII. The results revealed that Tyr-92 of PsbU, especially its aromatic ring, was essential for maintaining its function. From the crystal structure of PSII, Tyr-92 is located close to Pro-340 of D1, suggesting that the aromatic ring of Tyr-92 interacts with the CH group of Pro-340 of D1, and this CH/pi interaction is important for the optimal function of the Mn(4)Ca-cluster.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Okumura A,Sano M,Suzuki T,Tanaka H,Nagao R,Nakazato K,Iwai M,Adachi H,Shen JR,Enami Idoi
10.1016/j.febslet.2007.10.015subject
Has Abstractpub_date
2007-11-13 00:00:00pages
5255-8issue
27eissn
0014-5793issn
1873-3468pii
S0014-5793(07)01072-1journal_volume
581pub_type
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