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Spectroscopic evidence for the presence of an iron-sulfur center similar to Fx of Photosystem I inHeliobacillus mobilis

  • Group 4: FMO-Protein, Reaction Centers and Electron Transport
  • Regular Papers
  • Published:
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Abstract

Treatment of membranes ofHeliobacillus mobilis with high concentrations of the chaotropic agent urea resulted in the removal of the iron-sulfur centers FA and FB from the reaction center, as indicated by EPR spectra under strongly reducing conditions. In urea-treated membranes, transient absorption measurements upon a laser flash indicated a recombination between the photo-oxidized primary donor P798+ and a reduced acceptor with a time constant of 20 ms at room temperature. Benzylviologen, vitamin K-3 and methylene blue were found to accept electrons from the reduced acceptor efficiently. A differential extinction coefficient of 225–240 mM−1 cm−1 at 798 nm was determined from experiments in the presence of methylene blue. Transient absorption difference spectra between 400 and 500 nm in the presence and absence of artificial acceptors indicated that the electron acceptor involved in the 20 ms recombination has an absorption spectrum similar to that of an iron-sulfur center. This iron-sulfur center was assigned to be analogous to FX of Photosystem I. Our results provide evidence in support of the presence of FX in heliobacteria, which was proposed on the basis of the reaction center polypeptide sequence (Liebl et al. (1993) Proc. Natl. Acad. Sci. USA 90: 7124–7128). Implications for the electron transfer pathway in the reaction center of heliobacteria are discussed.

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Abbreviations

(B)Chl:

(bacterio)chlorophyll

Vit. K-3:

vitamin K-3 (menadione)

BV:

benzylviologen

MB:

methylene blue

PMS:

phenazine methosulfate

Hc. mobilis :

Heliobacillus mobilis

References

  • Blankenship RE (1992) Origin and early evolution of photosynthesis. Photosynth Res 33: 91–111

    Google Scholar 

  • Bergmann K and O'Konski CT (1963) A spectroscopic study of methylene blue monomer, dimer and complexes with montmorillonite. J Phys Chem 67: 2169–2177

    Google Scholar 

  • Brettel K (1988) Electron transfer from A1 − to an iron-sulfur center with t1/2=200 ns at room temperature in Photosystem 1. FEBS Lett 239: 93–98

    Google Scholar 

  • Brok M, Vasmel H, Horikx JTG and Hoff AJ (1985) Electron transport components ofHeliobacterium chlorum investigated by EPR spectroscopy at 9 and 35 GHz. FEBS Lett 194: 322–326

    Google Scholar 

  • Büttner M, Xie DL, Nelson H, Pinther W, Hauska G and Nelson N (1992) Photosynthetic reaction center genes in green sulfur bacteria and in Photosystem I are related. Proc Natl Acad Sci USA 89: 8135–8139

    Google Scholar 

  • Fischer M (1990) Photosynthetic electron transfer inHeliobacterium chlorum studied by EPR spectroscopy. Biochim Biophys Acta 1015: 471–481

    Google Scholar 

  • Fuller RC, Sprague SG, Gest H and Blankenship RE (1985) A unique photosynthetic reaction center fromHeliobacterium chlorum. FEBS Lett 182: 345–349

    Google Scholar 

  • Golbeck JH and Cornelius JM (1986) Photosystem I charge separation in the absence of centers A and B. I. Optical characterization of center ‘A2’ and evidence for its association with a 64-kDa peptide. Biochim Biophys Acta 849: 16–24

    Google Scholar 

  • Golbeck JH, Parrett KG, Mehari T, Jones KL and Brand JJ (1988a) Isolation of the intact Photosystem I reaction center core containing P700 and iron-sulfur center FX. FEBS Lett 228: 268–272

    Google Scholar 

  • Golbeck JH, Mehari T, Parrett KG and Ikegami I (1988b) Reconstitution of the Photosystem I complex from the P700 and FX containing reaction center core protein and the FA/FB polypeptide. FEBS Lett 240: 9–14

    Google Scholar 

  • Golbeck JM and Bryant DA (1991) Photosystem I. Curr Topics Bioenerg 16: 83–177

    Google Scholar 

  • Hiraishi A (1989) Occurrence of menaquinone as the sole isoprenoid quinone in the photosynthetic bacteriumHeliobacterium chlorum. Arch Microbiol 151: 378–379

    Google Scholar 

  • Kleinherenbrink FAM and Amesz J (1993) Stoichiometries and rates of electron transfer and charge recombination inHeliobacterium chlorum. Biochim Biophys Acta 1143: 77–83

    Google Scholar 

  • Kleinherenbrink FAM, Aartsma TJ and Amesz J (1991) Charge separation and formation of bacteriochlorophyll triplets inHeliobacterium chlorum. Biochim Biophys Acta 1057: 346–352

    Google Scholar 

  • Kleinherenbrink FAM, Ikegami I, Hiraishi A, Otte SCM and Amesz J (1993) Electron transfer in menaquinone-depleted membranes ofHeliobacterium chlorum. Biochim Biophys Acta 1142: 69–73

    Google Scholar 

  • Kleinherenbrink FAM, Hastings G, Wittmershaus BP and Blankenship RE (1994) Delayed fluorescence from Fe-S type reaction centers at low redox potential. Biochemistry 33: 3096–3105

    Google Scholar 

  • Ke B (1973) The primary electron acceptor of Photosystem I. Biochim Biophys Acta 301: 1–33

    Google Scholar 

  • Koike H and Katoh S (1982) Spectral features of the bound electron acceptor A2 of Photosystem I. Photochem Photobiol 35: 527–531

    Google Scholar 

  • Liebl U, Mockensturm-Wilson M, Trost JT, Brune DC, Blankenship RE and Vermaas W (1993) Single core polypeptide in the reaction center of the photosynthetic bacteriumHeliobacillus mobilis: Structural implications and relations to other Photosystems. Proc Natl Acad Sci USA 90: 7124–7128

    Google Scholar 

  • Lin S, Chiou HC, Kleinherenbrink FAM and Blankenship RE (1994) Time-resolved spectroscopy of energy and electron transfer processes in the photosynthetic bacteriumHeliobacillus mobilis. Biophys J: 66: 437–445

    Google Scholar 

  • Mathis P (1990) Compared structure of plant and bacterial photosynthetic reaction centers. Evolutionary implications. Biochim Biophys Acta 1018: 163–167

    Google Scholar 

  • McKay RB (1965) Visible absorption spectra of some cationic dyes in solution. Trans Faraday Soc 61: 1787–1799

    Google Scholar 

  • Miller M, Liu X, Snyder S, Thurnauer MC and Biggins J (1992) Photosynthetic electron-transfer reactions in the green sulfur bacteriumChlorobium vibrioforme: Evidence for the functional involvement of iron-sulfur redox centers on the acceptor side of the reaction center. Biochemistry 31: 4354–4363

    Google Scholar 

  • Nitschke W and Rutherford AW (1991) Photosynthetic reaction centers—variations on a common structural theme. Trends Biochem Sci 16: 241–245

    Google Scholar 

  • Nitschke W, Feiler U and Rutherford AW (1990a) Photosynthetic reaction center of green sulfur bacteria studied by EPR. Biochemistry 29: 3834–3842

    Google Scholar 

  • Nitschke W, Sétif P, Liebl U, Feiler U and Rutherford AW (1990b) Reaction center photochemistry ofHeliobacterium chlorum. Biochemistry 29: 11079–11088

    Google Scholar 

  • Nuijs AM, vanDorssen RJ, Duysens LNM and Amesz J (1985) Excited states and primary photochemical reactions in the photosynthetic bacteriumHeliobacterium chlorum. Proc Natl Acad Sci USA 82: 6865–6868

    Google Scholar 

  • Oh-oka H, Kakutani S, Matsubara H, Malkin R and Itoh S (1993) Isolation of the photoactive reaction center complex that contains three types of Fe-S centers and a cytochromec subunit from the green sulfur bacteriumChlorobium limicola f.thiosulfatophilum, strain Larsen. Plant Cell Physiol 34: 93–100

    Google Scholar 

  • Parrett KG, Mehari T, Warren P and Golbeck JH (1989) Purification and properties of the intact P-700 and FX containing Photosystem I core protein. Biochim Biophys Acta 973: 324–332

    Google Scholar 

  • Parrett KG, Mehari T and Golbeck JH (1990) Resolution and reconstitution of the cyanobacterial Photosystem I complex. Biochim Biophys Acta 1015: 341–352

    Google Scholar 

  • Prince RC, Gest H and Blankenship RE (1985) Thermodynamic properties of the photochemical reaction center ofHeliobacterium chlorum. Biochim Biophys Acta 810: 377–384

    Google Scholar 

  • Sétif P and Brettel K (1993) Forward electron transfer from phylloquinone A1 to iron-sulfur centers in spinach Photosystem I. Biochemistry 32: 7846–7854

    Google Scholar 

  • Smit HWJ, Amesz J and Van derHoeven MFR (1987) Electron transfer and triplet formation in membranes of the photosynthetic bacteriumHeliobacterium chlorum. Biochim Biophys Acta 893: 232–240

    Google Scholar 

  • Swarthoff T, Van derVeek-Horsley KM and Amesz J (1981) The primary charge separation, cytochrome oxidation and triplet formation in preparations from the green photosynthetic bacteriumProsthecochloris aestuarii. Biochim Biophys Acta 635: 1–12

    Google Scholar 

  • Trost JT and Blankenship RE (1989) Isolation of a photoactive photosynthetic reaction center core antenna complex fromHeliobacillus mobilis. Biochemistry 28: 9898–9904

    Google Scholar 

  • Trost JT, Brune DC and Blankenship RE (1992) Protein sequences and redox titrations indicate that the electron acceptors in reaction centers from heliobacteria are similar to Photosystem I. Photosynth Res 32: 11–22

    Google Scholar 

  • Van deMeent EJ, Kleinherenbrink FAM and Amesz J (1990) Purification and properties of an antenna-reaction center complex from heliobacteria. Biochim Biophys Acta 1015: 223–230

    Google Scholar 

  • Van deMeent EJ, Kobayashi M, Erkelens C, vanVeelen PA, Amesz J and Watanabe T (1991) Identification of 8(1)-hydroxychlorophylla as a functional reaction center pigment in heliobacteria. Biochim Biophys Acta 1058: 356–362

    Google Scholar 

  • Vos MH, Klaassen HE and VanGorkom HJ (1989) Electron transport inHeliobacterium chlorum whole cells studied by electroluminescence and absorbance difference spectroscopy. Biochim Biophys Acta 973: 163–169

    Google Scholar 

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Authors and Affiliations

  1. Department of Chemistry and Biochemistry, Arizona State University, 85287-1604, Tempe, AZ, USA

    Frank A. M. Kleinherenbrink, Hung-Cheng Chiou & Robert E. Blankenship

  2. Department of Botany, Arizona State University, 85287-1604, Tempe, AZ, USA

    Russell LoBrutto

  3. Center for the Study of Early Events in Photosynthesis, Arizona State University, 85287-1604, Tempe, AZ, USA

    Frank A. M. Kleinherenbrink, Hung-Cheng Chiou, Russell LoBrutto & Robert E. Blankenship

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  1. Frank A. M. Kleinherenbrink
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  2. Hung-Cheng Chiou
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  3. Russell LoBrutto
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  4. Robert E. Blankenship
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Kleinherenbrink, F.A.M., Chiou, HC., LoBrutto, R. et al. Spectroscopic evidence for the presence of an iron-sulfur center similar to Fx of Photosystem I inHeliobacillus mobilis . Photosynth Res 41, 115–123 (1994). https://doi.org/10.1007/BF02184151

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  • DOI: https://doi.org/10.1007/BF02184151

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