TY - JOUR
T1 - The N-terminal sequence of the extrinsic PsbP protein modulates the redox potential of Cyt b559 in photosystem II
AU - Nishimura, Taishi
AU - Nagao, Ryo
AU - Noguchi, Takumi
AU - Nield, Jon
AU - Sato, Fumihiko
AU - Ifuku, Kentaro
N1 - Funding Information:
This work was supported in part by JST PRESTO (K.I.), by JSPS KAKENHI (grant no. 26660087 to K.I.; 26840091 to R.N.; 24000018 and 25291033 to T.No.), and MEXT KAKENHI (grant no. 24107003 to T.No.). The JST CREST also contributed to this work (part to J.N.). T.Ni. is supported as a JSPS research fellow (grant no. 15J08254).
PY - 2016/2/18
Y1 - 2016/2/18
N2 - The PsbP protein, an extrinsic subunit of photosystem II (PSII) in green plants, is known to induce a conformational change around the catalytic Mn4CaO5 cluster securing the binding of Ca2+ and Cl- in PSII. PsbP has multiple interactions with the membrane subunits of PSII, but how these affect the structure and function of PSII requires clarification. Here, we focus on the interactions between the N-terminal residues of PsbP and the α subunit of Cytochrome (Cyt) b559 (PsbE). A key observation was that a peptide fragment formed of the first N-terminal 15 residues of PsbP, 'pN15', was able to convert Cyt b559 into its HP form. Interestingly, addition of pN15 to NaCl-washed PSII membranes decreased PSII's oxygen-evolving activity, even in the presence of saturating Ca2+ and Cl- ions. In fact, pN15 reversibly inhibited the S1 to S2 transition of the OEC in PSII. These data suggest that pN15 can modulate the redox property of Cyt b559 involved in the side-electron pathway in PSII. This potential change of Cyt b559, in the absence of the C-terminal domain of PsbP, however, would interfere with any electron donation from the Mn4CaO5 cluster, leading to the possibility that multiple interactions of PsbP, binding to PSII, have distinct roles in regulating electron transfer within PSII.
AB - The PsbP protein, an extrinsic subunit of photosystem II (PSII) in green plants, is known to induce a conformational change around the catalytic Mn4CaO5 cluster securing the binding of Ca2+ and Cl- in PSII. PsbP has multiple interactions with the membrane subunits of PSII, but how these affect the structure and function of PSII requires clarification. Here, we focus on the interactions between the N-terminal residues of PsbP and the α subunit of Cytochrome (Cyt) b559 (PsbE). A key observation was that a peptide fragment formed of the first N-terminal 15 residues of PsbP, 'pN15', was able to convert Cyt b559 into its HP form. Interestingly, addition of pN15 to NaCl-washed PSII membranes decreased PSII's oxygen-evolving activity, even in the presence of saturating Ca2+ and Cl- ions. In fact, pN15 reversibly inhibited the S1 to S2 transition of the OEC in PSII. These data suggest that pN15 can modulate the redox property of Cyt b559 involved in the side-electron pathway in PSII. This potential change of Cyt b559, in the absence of the C-terminal domain of PsbP, however, would interfere with any electron donation from the Mn4CaO5 cluster, leading to the possibility that multiple interactions of PsbP, binding to PSII, have distinct roles in regulating electron transfer within PSII.
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U2 - 10.1038/srep21490
DO - 10.1038/srep21490
M3 - Article
C2 - 26887804
AN - SCOPUS:84958559697
VL - 6
JO - Scientific Reports
JF - Scientific Reports
SN - 2045-2322
M1 - 21490
ER -