2005
DOI: 10.1021/bi047400+
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Influence of the 33 kDa Manganese-Stabilizing Protein on the Structure and Substrate Accessibility of the Oxygen-Evolving Complex of Photosystem II

Abstract: The 33 kDa manganese-stabilizing extrinsic protein binds to the lumenal side of photosystem II (PS II) close to the Mn 4 Ca cluster of the oxygen-evolving complex, where it limits access of small molecules to the metal site. Our previous finding that the removal of this protein did not alter the magnetic coupling regime within the manganese cluster, measured by electron spin-echo envelope modulation [Gregor, W., and Britt, R. D. (2000) Photosynth. Res. 65,[175][176][177][178][179][180][181][182][183][184][185… Show more

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Cited by 12 publications
(6 citation statements)
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“…However, 18 O exchange measurements of PSII samples in which the PsbO protein was biochemically removed did not show any significant increase in the exchange rates in the S 3 state, implying this was not a limiting kinetic property [40]. Similarly, ESEEM measurements of the proton couplings with the catalytic Mn in the S 1 state did not reveal any significant differences in PsbO-depleted samples [50]. However, it may be possible that excess Ca 2+ added for activity results in subtle conformational changes in PSII that recreates a kinetic protein barrier previously formed by the PsbO protein.…”
Section: Effect Of the Protein Environment On Substrate Water Exchangementioning
confidence: 86%
“…However, 18 O exchange measurements of PSII samples in which the PsbO protein was biochemically removed did not show any significant increase in the exchange rates in the S 3 state, implying this was not a limiting kinetic property [40]. Similarly, ESEEM measurements of the proton couplings with the catalytic Mn in the S 1 state did not reveal any significant differences in PsbO-depleted samples [50]. However, it may be possible that excess Ca 2+ added for activity results in subtle conformational changes in PSII that recreates a kinetic protein barrier previously formed by the PsbO protein.…”
Section: Effect Of the Protein Environment On Substrate Water Exchangementioning
confidence: 86%
“…[15,19,21,32,35,129,213] K-edge difference spectra from XANES measurements show that structural changes in the S 1 !S 2 transition, which involve oxidation of Mn III to Mn IV , are significantly different from changes in the S 2 !S 3 transition. [140,214] EXAFS data also point to a structural change between the S 2 and S 3 states, [20,42,49,203,[215][216][217][218] but different results have been reported from different studies. An equilibrium between at least two states in S 3 has been proposed by Renger.…”
Section: The S 1 !S 2 Transitionmentioning
confidence: 91%
“…647 EXAFS data point to a significant structural change between S 2 and S 3 , but different interpretations have been offered in different studies. 657,670,701,726,728,758,[770][771][772][773][774][775] It has also been proposed that there is an equilibrium between at least two states in S 3 . 677,770 From XANES measurements, K edge difference spectra for the S 1 f S 2 and S 2 f S 3 transitions are significantly different, with oxidation of Mn(III) to Mn(IV) occurring in the former.…”
Section: Coordination Of Asp170?mentioning
confidence: 99%