Aromatic structure of tyrosine-92 in the extrinsic PsbU protein of red algal photosystem II is important for its functioning.

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 Lett

journal_title

FEBS letters

authors

Okumura A,Sano M,Suzuki T,Tanaka H,Nagao R,Nakazato K,Iwai M,Adachi H,Shen JR,Enami I

doi

10.1016/j.febslet.2007.10.015

subject

Has Abstract

pub_date

2007-11-13 00:00:00

pages

5255-8

issue

27

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(07)01072-1

journal_volume

581

pub_type

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