Photosystem I
DOI: 10.1007/978-1-4020-4256-0_21
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Electrogenic Reactions Associated with Electron Transfer in Photosystem I

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Cited by 21 publications
(9 citation statements)
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“…Like in the case of the BRC (see Table 1), the ε value in the protein domain between the Chl (bacteriochlorophyll) dimer and Q A is the lowest, whereas it gradually increases at the donor side. A similar increase in the effective dielectric constant is observed at the donor side of PS I [11,12]. Note that the ε value in the domain between Y Z and P680 is only ~1.5 times higher than that at the P680-Q A region, while the ε values in the Pc-P700 and cyt c 559 -P960 protein regions of PS I and BRC, respectively, increase about threefold relative to the hydrophobic core domains (Tables 1 and 2), which is seemingly consistent with higher electron transfer rate (30 nsec [22]) compared to that at the donor sides of PS I and BRC (microsecond to millisecond lifetime range).…”
Section: Photosystem IIsupporting
confidence: 76%
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“…Like in the case of the BRC (see Table 1), the ε value in the protein domain between the Chl (bacteriochlorophyll) dimer and Q A is the lowest, whereas it gradually increases at the donor side. A similar increase in the effective dielectric constant is observed at the donor side of PS I [11,12]. Note that the ε value in the domain between Y Z and P680 is only ~1.5 times higher than that at the P680-Q A region, while the ε values in the Pc-P700 and cyt c 559 -P960 protein regions of PS I and BRC, respectively, increase about threefold relative to the hydrophobic core domains (Tables 1 and 2), which is seemingly consistent with higher electron transfer rate (30 nsec [22]) compared to that at the donor sides of PS I and BRC (microsecond to millisecond lifetime range).…”
Section: Photosystem IIsupporting
confidence: 76%
“…The lifetimes of the electron and proton transfer reactions on the acceptor side of BRC (submillisecond time range) are at least three orders of magnitude lower than those values at the domain of the iron sulfur clusters in PS I (range of tens to hundreds of nanoseconds). Perhaps, the three order of magnitude difference between the rate constants of charge transfer on the acceptor side of BRC and PS I, and threefold increase in the estimated value of ε reflects the hypothet ical correlation between the reaction rates and the dielec tric properties of the corresponding protein domains between redox cofactors suggested in our earlier works [11,12].…”
Section: Bacterial Reaction Centers and Photosystem Imentioning
confidence: 90%
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