The electron donor side of photosystem II: the oxygen evolving complex.
نویسندگان
چکیده
The 02-evolving complex (OEC) of photosynthesis resides near the inner side of the thylakoid membrane. Currently, it is believed to be composed of at least four polypeptides: (1) an intrinsic 27-34 kilodalton (kD) polypeptide that may be associated with manganese (Mn) ; (2) a peripheral 33 k D polypeptide, perhaps also associated with Mn; (3) a peripheral 24 kD polypeptide; and (4) a peripheral 18 kD polypeptide. At least three other polypeptides are associated with this complex to form Photosystem I1 (PSII): (1) a reaction center (RC) polypeptide, CP-47, of 47-51 kD molecular weight (M,) containing a chlorophyll a (P680), which is the primary electron donor, and a pheophytin (Pheo), which is the primary electron acceptor; also, a bound plastoquinol electron donor (Z), and a bound plastoquinone electron acceptor (aA) are suggested to be incorporated in this polypeptide; (2) a 32 kD polypeptide containing a second bound plastoquinone electron acceptor (QB); and (3) a 10 kD cytochrome (Cyt) b559, which exists in two forms: a high potential and a low potential. The primary reaction of PSI? the charge separation: P680.Pheo + hv .+ P680*Pheo-, in which the energy of a photon or an exciton is transformed to achieve the energetically uphill electron transfer. This electron is then transferred to the quinones on the reducing side of PSII. The oxidized reaction center (RC) chlorophyll (P680+) is reduced by removing an electron from Z, an event that can be observed
منابع مشابه
Oxygenic photosystem II: the mutation D1-D61N in Synechocystis sp. PCC 6803 retards S-state transitions without affecting electron transfer from YZ to P680+.
Photosynthetic oxygen evolution is powered by photosystem II (PSII), in particular by the oxidized chl a-aggregate P680+, and catalyzed by the oxygen-evolving complex (Mn4X-entity) as well as a tyrosine residue (YZ). The role of particular amino acids as cofactors of electron and proton transfer or as modulators of the activity is still ill-defined. The effects of single-site mutations at the d...
متن کاملPhotodamage to the oxygen evolving complex of photosystem II by visible light
Light damages photosynthetic machinery, primarily photosystem II (PSII), and it results in photoinhibition. A new photodamage model, the two-step photodamage model, suggests that photodamage to PSII initially occurs at the oxygen evolving complex (OEC) by light energy absorbed by manganese and that the PSII reaction center is subsequently damaged by light energy absorbed by photosynthetic pigme...
متن کاملEffect of an antiserum to a thylakoid membrane polypeptide on the primary photoreaction of photosystem II.
As was described previously, an antiserum to polypeptide 11000 inhibited photosynthetic electron transport on the oxygen evolving side of photosystem II. The effect of the antiserum on chloroplasts from two tobacco mutants also clearly showed that the inhibition site is on the photosystem II-side of the electron transport chain. One of the two tobacco mutants lacks the oxygen evolving capacity ...
متن کاملInhibition of photosynthetic electron transport in tobacco chloroplasts and thylakoids of the blue green alga Oscillatoria chalybea by an antiserum to synthetic zeaxanthin.
An antiserum to synthetic Zeaxanthin inhibits photosynthetic electron transport on the oxygen-evolving side of photosystem II in tobacco chloroplasts and thylakoids of the filamentous blue-green alga Oscillatoria chalybea. The inhibition site lies for both species between the site of electron donation of water or tetramethyl benzidine and that of diphenyl carbazide or manganese II ions. Typical...
متن کاملBicarbonate requirement for the water-oxidizing complex of photosystem II.
It is well established that bicarbonate stimulates electron transfer between the primary and secondary electron acceptors, Q(A) and Q(B), in formate-inhibited photosystem II; the non-heme Fe between Q(A) and Q(B) plays an essential role in the bicarbonate binding. Strong evidence of a bicarbonate requirement for the water-oxidizing complex (WOC), both O2 evolving and assembling from apo-WOC and...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Photochemistry and photobiology
دوره 42 2 شماره
صفحات -
تاریخ انتشار 1985