Skip to main content
SpringerLink
Log in

How is Ferredoxin-NADP Reductase Involved in the NADP Photoreduction of Chloroplasts?

  • Published:
Photosynthesis Research Aims and scope Submit manuscript

Abstract

NADP photoreduction of chloroplasts was discovered in 1951, and subsequent research was conducted to elucidate the enzymatic mechanisms involved in this reaction. In 1963, ferredoxin-NADP reductase (FNR; EC 1.18.1.2, ferredoxin-NADP oxidoreductase) was isolated and purified to a crystalline form. Because the reaction mechanism of ferredoxin-NADP reducing system was clarified in the isolated enzyme system, it was generally thought that the role of FNR in the NADP photoreduction of chloroplasts had been fully elucidated. However, the results of a reconstitution study using the crystallized FNR and the depleted grana, from which 'built-in' FNR had been eliminated, showed that the NADP photoreducing activity of reconstituted FNR was much lower than the original physiological activity, and as a result, more studies had to be continued. In 1985, a protein factor called ‘connectein’ was discovered, and it was shown that this new protein binds with two FNR molecules to form an FNR–connectein complex. Then in 1991, the FNR—connectein complex was formed using purified connectein and FNR, and after eliminating 'built-in' FNR, the reconstituted complex was bound to the depleted grana having reduced NADP photoreducing activity. The results showed that NADP photoreducing activity of the reconstituted system was comparable to the original physiological activity. This proved that the FNR—connectein complex, which binds to a specific site on the surface of thylakoid membrane, is functionally responsible for NADP photoreduction in chloroplasts.

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

References

  • Arnon DI (1951) Extracellular photosynthetic reactions. Nature 167: 1008–1010

    Article  PubMed  CAS  Google Scholar 

  • Arnon DI, Whatley FR and Allen MB (1957) Triphosphopyridine nucleotide as a catalyst of photosynthetic phosphorylation. Nature 180: 182–185

    Article  PubMed  CAS  Google Scholar 

  • Avron M and Jagendorf AT (1956) A TPNH diaphorase from chloroplasts. Arch Biochem Biophys 65: 475–490

    Article  PubMed  CAS  Google Scholar 

  • Avron M and Jagendorf AT (1957) Some further investigations on chloroplast TPNH diaphorase. Arch Biochem Biophys 72: 17–24

    Article  PubMed  CAS  Google Scholar 

  • Bookjans G, San Pietro A and Böger P (1978) Resolution and reconstitution of spinach ferredoxin-NADP+ reductase. Biochem Biophys Res Commun 80: 759–765

    Article  PubMed  CAS  Google Scholar 

  • Buchanan BB, Schürmann P, Wolosiuk RA and Jacquot J-P (2002) The ferredoxin/thioredoxin system: from discovery to molecular structures and beyond. Photosynth Res 73: 215–222

    Article  PubMed  CAS  Google Scholar 

  • Davenport HE (1963) Pathway of reduction of metmyoglobin and nicotinamide adenine dinucleotide phosphate by illuminated chloroplasts. Nature 199: 151–153

    Article  PubMed  CAS  Google Scholar 

  • Davenport HE, Hill R and Whatley FR (1952) A natural factor catalyzing reduction of methaemoglobin by isolated chloroplasts.Proc Roy Soc B 139: 346–358

    Article  CAS  Google Scholar 

  • Ellefson W and Krogmann DW (1979) Studies of the multiple forms of ferredoxin-NADP oxidoreductase from spinach. Arch Biochem Biophys 194: 593–599

    Article  PubMed  CAS  Google Scholar 

  • Forti G, Cappelletti A, Nobili RL, Garlaschi FM, Gerola PD and Jennings RC (1983) Interaction of ferredoxin and ferredoxin-NADP reductase with thylakoids. Arch Biochem Biophys 221: 507–513

    Article  PubMed  CAS  Google Scholar 

  • Foust GP, Mayhew SG and Massey V (1969) Complex formation between ferredoxin triphosphopyridine nucleotide reductase and electron transfer proteins. J Biol Chem 244: 964–970

    PubMed  CAS  Google Scholar 

  • Fredricks WW and Gehl JM (1976) Multiple forms of ferredoxinnicotinamide adenine dinucleotide phosphate reductase from spinach. Arch Biochem Biophys 174: 666–674

    Article  PubMed  CAS  Google Scholar 

  • Gewitz HS and Völker W (1962) Ñber die atmungsfermente der Chlorella. Hoppe Seylers Z Physiol Chem 330: 124–131

    PubMed  CAS  Google Scholar 

  • Gozzer C, Zannetti G, Galliano M, Sacchi GA, Minchiotti L and Curti B (1977) Molecular heterogeneity of ferredeoxin-NADP+ reductase from spinach leaves. Biochim Biophys Acta 485: 278–290

    PubMed  CAS  Google Scholar 

  • Hasumi H and Nakamur S (1978) Studies on the ferredoxin— ferredoxin-NADP reductase complex: kinetic and solvent perturbation studies on the location of sulfhydryl and aromatic amino acid residues. J Biochem 84: 707–717

    PubMed  CAS  Google Scholar 

  • Hasumi H, Nagata E and Nakamura S (1983) Molecular heterogeneity of ferredoxin-NADP+ reductase from spinach leaves.Biochem Biophys Res Commun 110: 280–286

    Article  PubMed  CAS  Google Scholar 

  • Jagendorf AT (2002) Photophosphorylation and the chemiosmotic perspective. Photosynth Res 73: 233–241

    Article  PubMed  CAS  Google Scholar 

  • Karplus PA, Walsh KA and Herriott JR (1984) Amino acid sequence of spinach ferredoxin:NADP+ oxidoreductase. Biochemistry 23: 6576–6583

    Article  PubMed  CAS  Google Scholar 

  • Ke B (2002) P430: a retrospective, 1971—2001. Photosynth Res 73: 207–214

    Article  Google Scholar 

  • Keirns JJ and Wang JH (1972) Studies on nicotinamide adenine dinucleotide phosphate reductase of spinach chloroplasts. J Biol Chem 247: 7374–7382

    PubMed  CAS  Google Scholar 

  • Keister DL, San Pietro A and Stolzenbach FE (1960) Pyridine nucleotide transhydro-genase from spinach. I. Purification and Properties. J Biol Chem 235: 2989–2996

    PubMed  CAS  Google Scholar 

  • Matthijs HCP, Coughlan SJ and Hind G (1986) Removal of ferredoxin: NADP+ oxidoreductase from thylakoid membranes, rebinding to depleted membranes, and identification of the binding site. J Biol Chem 261: 12154–12158

    PubMed  CAS  Google Scholar 

  • Melis A and Buchanan BB (eds) (1995) Special Issue: a tribute to Daniel I. Arnon. Photosynth Res 46: 1–376

  • Mortenson LE, Valentine RC, Carnahan JE (1962) An electron transport factor from Clostridium pasteurianum. Biochem Biophys Res Commun 7: 448–452

    Article  PubMed  CAS  Google Scholar 

  • Nakatani S and Shin M (1991) The reconstituted NADP photoreducting system by rebinding of the large form of ferredoxin-NADP reductase to depleted thylakoid membrane. Arch Biochem Biophys 291: 390–394

    Article  PubMed  CAS  Google Scholar 

  • Nelson N and Ben-Shem A (2002) Photosystem I reaction center: past and future. Photosynth Res 73: 193–206

    Article  PubMed  CAS  Google Scholar 

  • Nelson N and Neumann J (1969) Interaction between ferredoxin and ferredoxin nicotinamide adenine dinucleotide phosphate reductase in pyridine nucleotide photoreduction and some partial reactions. II. Complex formation between ferredoxin and ferredoxin-nicotinamide adenine dinucleotide phosphate reductase and its relevance to pyridine nucleotide photoreduction. J Biol Chem 244: 1932–1936

    PubMed  CAS  Google Scholar 

  • Nisikawa T, Sakai K, Sakihama N and Shin M (1992) Identification of ferredoxin-NADP reductase located at some inner part of thylakoid membranes. In: Murata N (ed) Research in Photosymtesis Vol II, pp 547–550. Kluwer Academic Publishers, Dordrecht, The Netherlands

    Google Scholar 

  • Nozaki Y, Tamaki M and Shin M (1985) The reconstituted NADP+ photoreducing system by recombination of ferredoxin-NADP+ reductase and connectein with thylakoids. Physiol Vég 23: 627–633

    CAS  Google Scholar 

  • Porra RJ (2002) The chequered history of the development and use of simultaneous equations for the accurate determination of chlorophylls a and b. Photosynth Res 73: 149–156

    Article  PubMed  CAS  Google Scholar 

  • Sakihama N, Nishimura I, Obata S and Shin M (1995) Mature ferredoxin-NADP reductase with a glutaminyl residue at N-terminus from spinach chloroplasts. Photosynth Res 46: 323–328

    Article  CAS  Google Scholar 

  • San Pietro A and Lang HM (1956) Accumulation of reduced pyridine nucleotides by illuminated grana. Science 124: 118–119

    CAS  Google Scholar 

  • San Pietro A and Lang HM (1958) Photosynthetic pyridine nucleotide reductase I. Partial purification and properties of the enzyme from spinach. J Biol Chem 231: 211–229

    PubMed  CAS  Google Scholar 

  • Schneeman R and Krogmann DW (1975) Polycation interactions with spinach ferredoxin-nicotinamide adenine dinucleotide phosphate reductase. J Biol Chem 250: 4965–4971

    PubMed  CAS  Google Scholar 

  • Shahak Y, Crowther D and Hind G (1981) The involvement of ferredoxin-NADP+ reductase in cyclic electron transport in chloroplasts. Biochim Biophys Acta 636: 234–243

    Article  PubMed  CAS  Google Scholar 

  • Sheriff S, Teller DC and Herriott JR (1980) Ferredoxin-NADP+ oxidoreductase is active as a monomer with molecular weight 33,000—36,000. Arch Biochem Biophys 205: 499–502

    Article  PubMed  CAS  Google Scholar 

  • Shin M (1990) Structure and function of ferredoxin-NADP reductase complex. In: Baltscheffsky (ed) Current Research in Photosynthesis Vol II, pp 659–662. Kluwer Academic Publishers, Dordrecht, The Netherlands

    Google Scholar 

  • Shin M and Arnon DI (1965) Enzymic mechanisms of pyridine nucleotide reduction in chloroplasts. J Biol Chem 240: 1405–1411

    PubMed  CAS  Google Scholar 

  • Shin M and Oshino R (1980) Isolation of two molecular forms of ferredoxin-NADP reductase from spinach. In: Yagi K and Yamano T (eds) Flavins and Flavoproteins, pp 537–541. Japan Scientific Societies Press, Tokyo and University Park Press, Baltimore, Maryland

    Google Scholar 

  • Shin M and Sakihama N (1984) On the nature of ferredoxin: ferredoxin-NADP reductase complex. In: Bray RC, Engel PC and Mayhew SG (eds) Flavins and Flavoproteins, pp 175–178. Walter de Gruyter, Berlin

    Google Scholar 

  • Shin M and San Pietro A (1968) Complex formation of ferredoxin-NADP reductase with ferredoxin and with NADP+. Biochem Biophys Res Commun 33: 38–42

    Article  PubMed  CAS  Google Scholar 

  • Shin M, Tagawa K and Arnon DI (1963) Crystallization of ferredoxin-TPN reductase and its role in the photosynthetic apparatus of chloroplasts. Biochem Z 338: 84–96

    PubMed  CAS  Google Scholar 

  • Shin M, Wakita R, Yamasaki Y and Oshino R (1981) Interrelation of two forms of ferredoxin-NADP+ reductase with different molecular weights. Plant Cell Physiol 22: 343–346

    CAS  Google Scholar 

  • Shin M, Ishida H and Nozaki Y (1985) A new protein factor, Connectein as a constituent of the large form of ferredoxin-NADP reductase. Plant Cell Physiol 26: 559–563

    CAS  Google Scholar 

  • Shin M, Tsujita M, Tomizawa H, Sakihama N, Kamei K and Oshino R (1990) Proteolytic degradation of ferredoxin-NADP reductase during purification from spinach. Arch Biochem Biophys 279: 97–103

    Article  PubMed  CAS  Google Scholar 

  • Tagawa K and Arnon DI (1962) Ferredoxins as electron carriers in photosynthesis and in the biological production and consumption of hydrogen gas. Nature 195: 537–543

    Article  PubMed  CAS  Google Scholar 

  • Tolmach LJ (1951) Effects of triphosphopyridine nucleotide upon oxygen evolution and carbon dioxide fixation by illuminated chloroplasts. Nature 167: 946–948

    Article  PubMed  CAS  Google Scholar 

  • Vishniac W and Ochoa S (1951) Photochemical reduction of pyridine nucleotides by spinach grana and coupled carbon dioxide fixation. Nature 167: 768–769

    Article  PubMed  CAS  Google Scholar 

  • Walker DA (2002) 'And whose bright presence'— an appreciation of Robert Hill and his reaction. Photosynth Res 73: 51–54

    Article  PubMed  CAS  Google Scholar 

  • Whatley FR and Arnon DI (1963) Photosynthetic phosphorylation in plants. In: Colowick SP and Kaplan NO (eds) Methods in Enzymol VI, pp 308–313. Academic Press, London

    Chapter  Google Scholar 

  • Yamasaki Y, Ishida H and Shin M (1983) Reassociation of the small form of ferredoxin-NADP+ reductase to the large form. Plant Cell Physiol 24: 1313–1316

    CAS  Google Scholar 

  • Zanetti G and Arosio P (1980) Solubilization from spinach thylakoids of a higher molecular weight form of ferredoxin-NADP+ reductase. FEBS Lett 111: 373–376

    Article  PubMed  CAS  Google Scholar 

  • Zanetti G and Forti G (1966) Studies on the triphosphopyridine nucleotide-cytochrome f reductase of chloroplasts. J Biol Chem 241: 279–285

    PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Teru Biolaboratory, 12-28, Sakurai-3, Mino-shi, Osaka, 562-0043, Japan

    Masateru Shin

Authors
  1. Masateru Shin
    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

Shin, M. How is Ferredoxin-NADP Reductase Involved in the NADP Photoreduction of Chloroplasts?. Photosynthesis Research 80, 307–313 (2004). https://doi.org/10.1023/B:PRES.0000030456.96329.f9

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1023/B:PRES.0000030456.96329.f9

Search

Navigation