The peculiarities of the electron transfer from cytochrome to the cation-radical of bacteriochlorophyll dimer in reaction centers from Rps. viridis
β Scribed by Fyodor I. Dalidchik; Eugen N. Frolov; Vitalii I. Goldanskii
- Publisher
- Elsevier Science
- Year
- 1994
- Tongue
- English
- Weight
- 349 KB
- Volume
- 223
- Category
- Article
- ISSN
- 0009-2614
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β¦ Synopsis
The kinetics of tunnel electron transitions in reaction centers of photosynthetic bacteria Rkodopseudomonas viridis are characterized by paradoxical peculiarities. ( 1) The time of the high-temperature (300 K) transfer of an electron to the cation-radical of bacteriochlorophyll BCl: from the neigbbour heme C 38c is almost twice as long as that from the almost .twice as distant heme C, (2) At low temperature (77 K) the majority (~~80%) of nearby hemes C rsc is unable to reduce BCl$ while all remote hemes Czc participate effectively in such reductions as though they disconnect C 3W hemes. Both these peculiarities find their explanation on the basis of the mechanism of two-electron relay tunneling: C380+C-BCl$, CzD+c-C3+80.
π SIMILAR VOLUMES
Spectral and kinetic characteristics of fluorescence from isolated reaction centers of photosynthetic purple bacteria Rhodobacter sphaeroides and Rhodobacter capsulatus were measured at room temperature under rectangular shape of excitation at 810 nm. The kinetics of fluorescence at 915 nm reflected
We have measured the extent of flash-induced electron transfer from the bacteriochlorophyll dimer, P, to the bacteriopheophytin in the M-subunit, HM, in reaction centers of Rhodopseudomonas viridis. This has been done by measuring the transient states produced by excitation of reaction centers trapp