Skip to main content
SpringerLink
Log in

Redox effects on the bacteriochlorophyll α-containing Fenna-Matthews-Olson protein fromChlorobium tepidum

  • Group 4: FMO-Protein, Reaction Centers and Electron Transport
  • Regular Papers
  • Published:
Photosynthesis Research Aims and scope Submit manuscript

Abstract

The BChla-containing Fenna-Matthews-Olson (FMO) protein from the green sulfur bacteriumChlorobium tepidum was purified and characterized. Fluorescence spectra indicate that efficient excited state quenching occurs at neutral or oxidizing redox potentials. The major fluorescence lifetime at room temperature is approximately 60 ps in samples that are in neutral or oxidizing conditions, and approximately 2 ns in samples where the strong reductant sodium dithionite has been added. A similar change is observed in pump-probe picosecond absorbance difference experiments, where the long life time component increases after dithionite addition. A 16 Gauss wide EPR signal with g factor =2.005 is observed in samples without dithionite. This signal largely disappears upon addition of dithionite. Dithionite induces large reversibile changes in the 77 K absorbance spectra of the purified FMO protein and in whole cells. These results indicate that the FMO protein contains redox active groups, which may be involved in the regulation of energy transfer. Room temperature circular dichroism and low temperature absorption spectra show that dithionite also induces conformational or structural changes of the FMO protein complex.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

Abbreviations

BChl:

bacteriochlorophyll

FMO protein:

Fenna-Matthews-Olson protein

References

  • Babcock GT, El-Deeb MK, Sandusky PO, Whittaker MM and Whittaker JW (1992) Electron paramagnetic resonance and electron nuclear double resonance spectroscopies of the radical site in galactose oxidase and of thioether-substituted phenol model compounds. J Am Chem Soc 114: 3727–3734

    Google Scholar 

  • Barry BA and Babcock GT (1987) Tyrosine radicals are involved in the photosynthetic oxygen-evolving system. Proc Natl Acad Sci USA 84: 7099–7103

    Google Scholar 

  • Blankenship RE (1985) Electron transport in green photosynthetic bacteria. Photosynth Res 6: 317–333

    Google Scholar 

  • Blankenship RE, Cheng P, Causgrove TP, Brune DC, Wang SH, Choh JU and Wang J (1993) Redox regulation of energy transfer efficiency in antennas of green photosynthetic bacteria. Photochem Photobiol 57: 103–107

    Google Scholar 

  • Blankenship RE, Wang J, Causgrove TP and Brune DC (1990) Efficiency and kinetics of energy transfer in chlorosome antennas from green photosynthetic bacteria. In: Baltscheffsky M (ed) Current Research in Photosynthesis, Vol II, pp 17–24. Kluwer Academic Publishers, Dordrecht, The Netherlands

    Google Scholar 

  • Borg DC, Forman A and Fajer J (1976) ESR and ENDOR studies of the cation radical of bacteriochlorophyll. J Am Chem Soc 95: 6889–6893

    Google Scholar 

  • Causgrove TP, Brune DC, Wang J, Wittmershaus BP and Blankenship RE (1990) Energy transfer kinetics in whole cells and isolated chlorosome of green photosynthetic bacteria. Photosynth Res 26: 39–48

    Google Scholar 

  • Cheng P (1992) Characterization of energy transfer and structure of the antenna system of green photosynthetic bacteria. PhD dissertation. Arizona State University, Tempe, AZ

  • Daurat-Larroque ST, Brew K and Fenna RE (1986) The complete amino acid sequence of a bacteriochlorophylla-protein fromProsthecochloris aestuarii. J Biol Chem 261: 3607–3615

    Google Scholar 

  • Davidson VL and Jones LH (1992) Cofactor-directed inactivation by nucleophilic amines of the quinoprotein methylamine dehydrogenase fromParacoccus denitrificans. Biochim Biophys Acta 1121: 104–110

    Google Scholar 

  • Davis FS, Nemeth GA, Anjo DM, Makings LR, Gust D and Moor TA (1987) Digital back-off for computer controlled flash spectrometers. Rev Sci Inst 58: 1629–1631

    Google Scholar 

  • Dracheva S, Williams JC and Blankenship RE (1992) Cloning and sequencing of the FMO-protein gene fromChlorobium tepidum. In: Murata N (ed) Research in Photosynthesis, Vol I, pp 53–56. Kluwer Academic Publishers, Dordrecht, The Netherlands

    Google Scholar 

  • Johnson SG and Small GJ (1991) Excited-state structure and energytransfer dynamics of the bacteriochlorophylla antenna complex fromProsthecochloris aestuarii. J Phys Chem 95: 471–479

    Google Scholar 

  • Karapetyan NV, Swarthoff T, Rijgersberg CP and Amesz J (1980) Fluorescence emission spectra of cells and subcellular preparations of a green photosynthetic bacterium, effects of dithionite on the intensity of the emission bands. Biochim Biophys Acta 593: 254–260

    Google Scholar 

  • Kelly JM and Porter G (1970) The interaction of photo-excited chlorophylla with duroquinone, α-tocopherylquinone and vitamin K1. Proc R Soc London Ser A 319: 319–329

    Google Scholar 

  • Knutson JR, Beeche JM and Brand L (1983) Simultaneous analysis of multiple fluorescence decay curves: A global approach. Chem Phys Lett 102: 501–507

    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 

  • Lu XY and Pearlstein RM (1993) Simulations ofProsthecochloris bacteriochlorophylla-protein optical spectra improved by parametric computer search. Photochem Photobiol 57: 86–91

    Google Scholar 

  • Matthews BW and Fenna R (1980) Structure of a green bacteriochlorophyll protein. Acc Chem Res 13: 309–317

    Google Scholar 

  • Natarajan LV and Blankenship RE (1983) Free energy dependence of the quenching of chlorophylla fluorescence by substituted quinones. Photochem Photobiol 37: 329–336

    Google Scholar 

  • Olson JM (1978) Bacteriochlorophylla-proteins from green bacteria. In: Clayton RK and Sistrom WR (eds) The Photosynthetic Bacteria, pp 161–178. Plenum, New York

    Google Scholar 

  • Olson JM (1980) Bacteriochlorophylla-proteins of two green photosynthetic bacteria. Meth Enzymol 69: 336–344

    Google Scholar 

  • Olson JM, Ke B and Thompson KH (1976) Exciton interaction among chlorophyll molecules in bacteriochlorophylla proteins and bacteriochlorophylla reaction center complexes from green bacteria. Biochim Biophys Acta 430: 524–537

    Google Scholar 

  • Olson JM, Ormerod JG, Amesz J, Stackebrandt E and Trüper HG (eds) (1988) Green photosynthetic Bacteria. Plenum, New York

    Google Scholar 

  • Olson JM, Philipson KD and Sauer K (1973) Circular dichroism and absorption spectra of bacteriochlorophyll-protein and reaction center complexes fromChlorobium thiosulfatophilum. Biochim Biophys Acta 292: 206–217

    Google Scholar 

  • Orme-Johnson WH and Beinert H (1969) On the formation of the superoxide anion radical during the reaction of reduced ironsulfur proteins with oxygen. Biochem Biophys Res Comm 36: 905–9114

    Google Scholar 

  • Paz MA, Fluckiger R, Boak A, Kagan HM and Gallop PM (1991) Specific detection of quinoproteins by redox-cycling staining. J Biol Chem 266: 689–692

    Google Scholar 

  • Pearlstein RM (1992) Theory of the optical spectra of the bacteriochlorophylla antenna protein trimer fromProsthecochloris aestuarii. Photosynth Res 31: 213–226

    Google Scholar 

  • Philipson KD and Sauer K (1972) Excitation interaction in a bacteriochlorophyll-protein from Chloropseudomonas ethylica. Absorption and circular Dichroism at 77 °K. Biochemistry 11: 1880–1885

    Google Scholar 

  • Savikhin S, Zhou W, Blankenship RE and Struve WS (1994) Femtosecond energy transfer and spectral equilibration in FMO trimers from the green bacteriumChlorobium tepidum. Biophys J in press

  • Tronrud DE, Schmid MF and Matthews BW (1986) Structure and X-ray amino acid sequence of a bacteriochlorophylla protein fromProsthecochloris aestuarii refined at 1.9 Å resolution. J Mol Biol 188: 443–454

    Google Scholar 

  • Tronrud DE and Matthews BW (1993) Refinement of the Structure of a Water-Soluble Antenna Complex from Green Photosynthetic Bacteria by Incorporation of the Chemically Determined Amino Acid Sequence. In: Norris J and Deisenhofer J (eds) The Photosynthetic Reaction Center, Vol 1, pp 13–21. Academic Press, San Diego, CA

    Google Scholar 

  • VanGrondelle R (1985) Excitation energy transfer, trapping and annihilation in photosynthetic systems Biochim Biophys Acta 811: 147–195

    Google Scholar 

  • VanMourik F, Verwijst RR, Mulder JM and VanGrondelle R (1993) Excitation transfer dynamics and spectroscopic properties of the light-harvesting BChla complex ofProsthecochloris aestuarii. J Lumin 53: 499–502

    Google Scholar 

  • Van Mourik F (1993) Spectral inhomogeneity of the bacterial lightharvesting antennae: Causes and consequences. PhD thesis, Free University, Amsterdam, The Netherlands

  • Vos M, Nuijs AM, VanGrondelle R, VanDorssen RJ, Gerola PD and Amesz J (1987) Excitation transfer in chlorosomes of green photosynthetic bacteria. Biochim Biophys Acta 891: 275–285

    Google Scholar 

  • Wang J, Brune DC and Blankenship RE (1990) Effects of oxidants and reductants on the efficiency of excitation transfer in green photosynthetic bacteria. Biochim Biophys Acta 1015: 457–463

    Google Scholar 

  • Whittaker MM and Whittaker JW (1990) A tyrosine-derived free radical in apogalactose oxidase. J Biol Chem 265: 9610–9613

    Google Scholar 

  • Whitten W, Olson JM and Pearlstein RM (1980) Seven-fold exciton splitting of the 810 nm band in bacteriochlorophylla-proteins from green photosynthetic bacteria. Biochim Biophys Acta 591: 203–207

    Google Scholar 

Download references

Author information

Authors and Affiliations

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

    Wenli Zhou, Su Lin & 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

    Wenli Zhou, Russell LoBrutto, Su Lin & Robert E. Blankenship

Authors
  1. Wenli Zhou
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Russell LoBrutto
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Su Lin
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Robert E. Blankenship
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Zhou, W., LoBrutto, R., Lin, S. et al. Redox effects on the bacteriochlorophyll α-containing Fenna-Matthews-Olson protein fromChlorobium tepidum . Photosynth Res 41, 89–96 (1994). https://doi.org/10.1007/BF02184148

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF02184148

Key words

Search

Navigation