Electrogenicity accompanies photoreduction of the iron-sulfur clusters F(A) and F(B) in photosystem I.

نویسندگان

  • M D Mamedov
  • K N Gourovskaya
  • I R Vassiliev
  • J H Golbeck
  • Sememov AYu
چکیده

Photovoltage responses accompanying electron transfer on the acceptor side of photosystem I (PS I) were investigated in proteoliposomes containing PS I complexes from the cyanobacterium Synechococcus sp. PCC 6301 using a direct electrometrical technique. The relative contributions of the F(X) --> F(B) and the F(X) --> F(A) electron transfer reactions to the overall electrogenicity were elucidated by comparing the sodium dithionite-induced decrease in the magnitude of the total photoelectric responses in control and in F(B)-less (HgCl2-treated) PS I complexes. The results obtained suggest that the electrogenesis on the acceptor side of PS I is related to electron transfers between both F(X) and F(A) and F(A) and F(B). Based on the electrogenic nature of the latter reaction in PS I complexes, we conclude that F(A) rather than F(B) is the acceptor proximal to F(X).

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

The structure of genetically modified iron-sulfur cluster F(x) in photosystem I as determined by X-ray absorption spectroscopy.

Photosystem I (PS I) mediates light-induced electron transfer from P700 through a chlorophyll a, a quinone and a [4Fe-4S] iron-sulfur cluster F(X), located on the core subunits PsaA/B to iron-sulfur clusters F(A/B) on subunit PsaC. Structure function relations in the native and in the mutant (psaB-C565S/D566E) of the cysteine ligand of F(X) cluster were studied by X-ray absorption spectroscopy ...

متن کامل

Assembly of photosystem I. II. Rubredoxin is required for the in vivo assembly of F(X) in Synechococcus sp. PCC 7002 as shown by optical and EPR spectroscopy.

The rubA gene was insertionally inactivated in Synechococcus sp. PCC 7002, and the properties of photosystem I complexes were characterized spectroscopically. X-band EPR spectroscopy at low temperature shows that the three terminal iron-sulfur clusters, F(X), F(A), and F(B), are missing in whole cells, thylakoids, and photosystem (PS) I complexes of the rubA mutant. The flash-induced decay kine...

متن کامل

Recruitment of a foreign quinone into the A1 site of photosystem I. Consecutive forward electron transfer from A0 TO A1 to FX with anthraquinone in the A1 site as studied by transient EPR.

In photosystem I (PS I), phylloquinone (PhQ) acts as a low potential electron acceptor during light-induced electron transfer (ET). The origin of the very low midpoint potential of the quinone is investigated by introducing anthraquinone (AQ) into PS I in the presence and absence of the iron-sulfur clusters. Solvent extraction and reincubation is used to obtain PS I particles containing AQ and ...

متن کامل

Appearance of Membrane-bound Iron-Sulfur Centers and the Photosystem I Reaction Center during Greening of Barley Leaves.

Dark-grown barley (Hordeum vulgare) etioplasts were examined for their content of membrane-bound iron-sulfur centers by electron paramagnetic resonance spectroscopy at 15K. They were found to contain the high potential iron-sulfur center characterized (in the reduced state) by an electron paramagnetic resonance g value of 1.89 (the "Rieske" center) but did not contain any low potential iron-sul...

متن کامل

Benzofuroxan as Electron Acceptor at Photosystem I

The midpoint potential of B F O . the sensitivity of its photoreduction to D C M U . D BM IB and K CN . and the photosystem I activity, suggest that the photoreduction of BFO in the chloroplast is at the primary electron acceptor x of photosystem I, and is irreversible. Rates of electron transport are similar in basal phosphorylating or uncoupled conditions al­ though electron transport is coup...

متن کامل

ذخیره 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 نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • FEBS letters

دوره 431 2  شماره 

صفحات  -

تاریخ انتشار 1998