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pH-dependent charge equilibria between tyrosine-D and the S states in photosystem II. Estimation of relative midpoint redox potentials.

Abstract：

:The effect of protonation events on the charge equilibrium between tyrosine-D and the water-oxidizing complex in photosystem II has been studied by time-resolved measurements of the EPR signal IIslow at room temperature. The flash-induced oxidation of YD by the water-oxidizing complex in the S2 state is a monophasic process above pH 6.5 and biphasic at lower pHs, showing a slow and a fast phase. The half-time of the slow phase increases from about 1 s at pH 8.0 to about 20 s at pH 5.0, whereas the half-time of the fast phase is pH independent (0.4-1 s). The dark reduction of YD+ was followed by measuring the decay of signal IIslow at room temperature. YD+ decays in a biphasic way on the tens of minutes to hours time scale. The minutes phase is due to the electron transfer to YD+ from the S0 state of the water-oxidizing complex. The half-time of this process increases from about 5 min at pH 8.0 to 40 min at pH 4.5. The hours phase of YD+ has a constant half-time of about 500 min between pH 4.7 and 7.2, which abruptly decreases above pH 7.2 and below pH 4.7. This phase reflects the reduction of YD+ either from the medium or by an unidentified redox component of PSII in those centers that are in the S1 state. The titration curve of the half-times for the oxidation of YD reveals a proton binding with a pK around 7.3-7.5 that retards the electron transfer from YD to the water-oxidizing complex. We propose that this monoprotic event reflects the protonation of an amino acid residue, probably histidine-190 on the D2 protein, to which YD is hydrogen bonded. The titration curves for the oxidation of YD and for the reduction of YD+ show a second proton binding with pK approximately 5.8-6.0 that accelerates the electron transfer from YD to the water-oxidizing complex and retards the process in the opposite direction. This protonation most probably affects the water-oxidizing complex. From the measured kinetic parameters, the lowest limits for the equilibrium constants between the S0YD+ and the S1YD as well as between the S1YD+ and S2YD states were estimated to be 5 and 750-1000, respectively.(ABSTRACT TRUNCATED AT 400 WORDS)

journal_name

Biochemistry

journal_title

Biochemistry

authors

Vass I,Styring S

doi

10.1021/bi00217a037

subject

Has Abstract

pub_date

1991-01-22 00:00:00

pages

830-9

issue

eissn

0006-2960

issn

1520-4995

journal_volume

pub_type

杂志文章

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pH-dependent charge equilibria between tyrosine-D and the S states in photosystem II. Estimation of relative midpoint redox potentials.