Skip to main content

Advertisement

SpringerLink
Log in

Memories: from protein synthesis to photosynthesis

  • Personal Perspective
  • Published:
Photosynthesis Research Aims and scope Submit manuscript

Abstract

Emphasis herein is on the early years of my scientific life, primarily in graduate school and at the McCollum-Pratt Institute, Johns Hopkins University, as techniques learned and research performed then became the basis for future scientific endeavors. Studies on the mechanism of conversion of light energy into chemical free energy were a logical consequence of earlier investigations on enzyme-catalyzed hydrogen transfer reactions and pyridine nucleotide coenzyme biochemistry. Identification of several protein factors involved in pyridine nucleotide reduction by illuminated chloroplasts is described and, hopefully, adequately and honestly referenced to complementary research in other laboratories. Coupled with progress were changes in nomenclature of the protein factors and are so noted. In particular, David Wharton proposed the descriptive name, ferredoxin, for the non-heme iron and labile sulfide-containing proteins which serve as redox cofactors in a variety of energy conserving reactions. The inclusion of “Lessons” is adapted from Efraim Racker (1976, A new look at mechanisms in bioenergetics. Academic Press, NY). They are lessons that I learned and are included herein solely for graduate students.

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

Fig. 1
Fig. 2
Fig. 3
Fig. 4
Fig. 5
Fig. 6
Fig. 7

Notes

  1. Our 1958 paper was designated a Classic Paper in Biochemistry—a series of papers reprinted to celebrate the centenary of the Journal of Biochemistry (JBC Vol. 280, No. 51, December 23, p. e48, 2005). An unexpected honor.

  2. The use of NAD rather than NADP in our experiments was dictated by price. My recollection is that the cost of NADP was about $1000 per gram; in contrast, the cost of NAD was only about $50 per gram.

  3. NAD, DPN, and Coenzyme I are one and the same as are NADP, TPN, and Coenzyme II.

  4. For a list of titles of other conferences, see Govindjee (2005).

  5. For a Timeline of research in oxygenic photosynthesis, see Govindjee and Krogmann (2005).

References

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

    Article  PubMed  CAS  Google Scholar 

  • Arnon DI, Allen MB, Whaley FR (1954a) Photosynthesis by isolated chloroplasts. Nature 174:394–396

    Article  PubMed  CAS  Google Scholar 

  • Arnon DI, Allen MB, Whatley FR (1954b) Photosynthesis by isolated chloroplasts. II Photophosphorylation, the conversion of light into phosphate bond energy. J Am Chem Soc 76:6324–6329

    Article  CAS  Google Scholar 

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

    Article  PubMed  CAS  Google Scholar 

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

    Article  PubMed  CAS  Google Scholar 

  • Bendall D (1994) Robert Hill. Biographical Memoirs of fellows of the Royal Society 40:141–171

  • Breslow R (1957) Rapid deuterium exchange in thiazolium salts. J Am Chem Soc 79:1762–1762

    Article  CAS  Google Scholar 

  • Burton RM, San Pietro A, Kaplan NO (1957) Preparation of pyridine nucleotide analogs by the carbonyl addition reaction. Arch Biochem Biophys 70:87–106

    Article  PubMed  CAS  Google Scholar 

  • Chance B, San Pietro A (1963) On the light-induced bleaching of photosynthetic pyridine nucleotide reductase in the presence of chloroplasts. Proc Natl Acad Sci USA 49:633–638

    Google Scholar 

  • Frenkel A (1954) Light-induced phosphorylation by cell free preparations of photosynthetic bacteria. J Am Chem Soc 76:5568–5569

    Article  CAS  Google Scholar 

  • Fry KT, San Pietro A (1962) Studies on photosynthetic pyridine nucleotide reductase. Biochem Biophys Res Commun 9:218–222

    Article  PubMed  CAS  Google Scholar 

  • Govindjee (2005) A list of photosynthesis conferences and of edited books in photosynthesis. In: Govindjee, Beatty JT, Gest H, Allen JF (eds) Discoveries in photosynthesis. Springer, Dordrecht, pp 1249–1262

  • Govindjee, Krogmann D (2005) Discoveries in oxygenic photosynthesis (1727–2003): a perspective. In: Govindjee, Beatty JT, Gest H, Allen JF (eds) Discoveries in photosynthesis. Springer, Dordrecht, pp 63–105

  • Hill R, San Pietro A (1963) Hydrogen transport with chloroplasts. Zeit für Naturforschung 18b:677–682

    CAS  Google Scholar 

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

    PubMed  CAS  Google Scholar 

  • Keister DL, San Pietro A, Stolzenbach FE (1962) Pyridine nucleotide transhydrogenase from spinach, II. Requirement of enzyme for photochemical accumulation of reduced pyridine nucleotides. Arch Biochem Biophys 98:235–244

    Article  PubMed  CAS  Google Scholar 

  • Lazzarini RA, San Pietro A (1962) The reduction of Cytochrome c by photosynthetic pyridine nucleotide reductase and transhydrogenase. Biochem Biophys Acta 62:417–420

    Article  PubMed  CAS  Google Scholar 

  • Peck HD, San Pietro A, Gest H (1956) On the mechanism of hydrogenase action. Proc Natl Acad Sci USA 42:13–19

    Article  PubMed  CAS  Google Scholar 

  • Pullman ME, San Pietro A, Colowick SP (1954) On the structure of reduced diphospho-pyridine nucleotide. J Biol Chem 206:129–141

    PubMed  CAS  Google Scholar 

  • Racker E (1976) A new look at mechanisms in bioenergetics. Academic Press, NY

    Google Scholar 

  • San Pietro A (1952) Synthesis of aspartic acid – 2,3-C14-N15 and its conversion to uric acid in the pigeon. J Biol Chem 198:639–642

    PubMed  CAS  Google Scholar 

  • San Pietro A (1955a) On the structure of the diphosphopyridine nucleotide-cyanide complex. J Biol Chem 217:579–587

    PubMed  CAS  Google Scholar 

  • San Pietro A (1955b) Base catalyzed deuterium exchange with diphosphopyridine nucleotide. J Biol Chem 217:589–593

    PubMed  CAS  Google Scholar 

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

    Article  CAS  Google Scholar 

  • San Pietro A, 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 

  • San Pietro A, Rittenberg D (1953a) Study of the rate of protein synthesis in humans: I measurement of the urea pool and urea space. J Biol Chem 201:445–456

    PubMed  CAS  Google Scholar 

  • San Pietro A, Rittenberg D (1953b) Study of the rate of protein synthesis in humans; II Measurement of the metabolic pool and the rate of protein synthesis. J Biol Chem 201:457–473

    PubMed  CAS  Google Scholar 

  • Tagawa K, 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) Effect of triphosphopyridine nucleotide upon oxygen evolution and carbon dioxide fixation by illuminated chloroplasts. Nature 167:946–948

    Article  PubMed  CAS  Google Scholar 

  • Vernon LP (2005) Photosynthesis and the Charles F. Kettering research laboratory. In: Govindjee, Beatty JT, Gest H, Allen JF (eds) Discoveries in photosynthesis. Springer, Dordrecht, pp 1133–1142

    Chapter  Google Scholar 

  • Vishniac W, 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 

  • Watson JD, Crick FHC (1953) A structure for deoxyribose nucleic acid. Nature 171:737–738

    Article  PubMed  CAS  Google Scholar 

Download references

Acknowledgment

It is my sincere pleasure to recall the many fine contributions of the students and scientists identified herein with whom I have collaborated during my scientific career. I have learned from each and every one of them and hope they feel they have benefited from our collaboration. I also thank Clanton C. Black and Bob Buchanan for reading this perspective, and Govindjee for inviting and editing this manuscript.

Author information

Authors and Affiliations

  1. Department of Biology, Indiana University, 1001 East Third Street, Bloomington, IN, 47405-3700, USA

    Anthony San Pietro

Authors
  1. Anthony San Pietro
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Anthony San Pietro.

Additional information

This perspective was invited and gratefully edited by Govindjee. I thank him for his patience over several years, for his understanding, for his hard work and for excellent editorial suggestions. At his request, a portrait of mine is included in this perspective.

Appendices

Appendix 1

A role of non-heme iron proteins in energy conversion

The ubiquity of the non-heme iron, labile sulfide-containing proteins in biological systems, and their role in energy conversion processes was only beginning to be realized in the mid-1960s. The initial discovery of the bacterial and plant ferredoxins in the 1950s focused primarily on their role in electron transport. The bacterial and plant ferredoxins are relatively simple proteins of low molecular weight (<20,000) and have no other detectable cofactors. The discovery of more complex non-heme iron proteins with higher molecular weights (>20,000) and which contain cofactors, such as flavins, and Coenzyme Q, was coincident with their role in energy conserving processes. By the mid-1960s, non-heme iron proteins were shown to function in mitochondrial electron transport and nitrogen fixation as well as photosynthetic electron transport. Clearly, the importance of non-heme iron proteins was beginning to approach that of the heme proteins. I believe the current view is that they are equally important.

I was fortunate to convene a symposium in 1965 entitled “Non-Heme Iron Proteins: Role in Energy Conversion.” Prior to the time of this symposium the problem of energy conversion was hardly even mentioned mainly because the focus earlier (1950s) had been on the simple bacterial and plant proteins. The more recent (early 1960s) research dealt with complex non-heme iron proteins such as aldehyde oxidase, which contains ubiquinone-Coenzyme Q, flavin, iron, labile sulfide, and molybdenum. This enzyme was proposed as a model for the electron transport chain in mitochondria because its susceptibility to inhibitors such as amytal, antimycin, and oligomycin is reminiscent of oxidative phosphorylation in mitochondria.

The late Professor Efraim (Ef) Racker, a pre-eminent biochemist, chaired the last session of the symposium and ended his Chairman’s Remarks as follows: “This morning we shall hear from Dr. Butow that there is a non-heme iron linked electron transport system in mitochondria which appears to be closely linked to the process of oxidative phosphorylation. Indeed, it begins to look as if non-heme iron (NHI) may become almost as important to studies of energy conversions as NIH. The remarkable vision of the organizer of this symposium who selected the title before a direct relationship between non-heme iron proteins and energy conversion was established must be admired.” As the sole organizer of that symposium, I was, and will always be, grateful to Ef Racker for his kind and gracious remark!

Appendix 2

Examples of some publications from the Kettering Research Laboratory (arranged chronologically) are:

  • Gest H, San Pietro A, Vernon LP (eds) (1963) Bacterial Photosynthesis. Antoioch Press, Yellow Springs, Ohio

  • Fry KT, Lazzarini RA, San Pietro A (1963) The photoreduction of iron in photosynthetic pyridine nucleotide reductase. Proc Natl Acad Sci USA 50:652–657

  • Black C C, San Pietro A, Norris G, Limbach D (1964) Photosynthetic phosphorylation in the presence of spinach phosphodoxin. Plant Physiol 39:279–283

  • San Pietro A (ed) (1965) Non-heme iron proteins: Role in energy conversion. Antioch Press, Yellow Springs, OH

  • San Pietro A, Black CC (1965) Enzymology of energy conversion in photosynthesis. Ann Rev Plant Physiol 16:155–174

  • Evans WR, San Pietro A (1966) Phosphorolysis of adenosine diphosphoribose. Arch Biochem Biophys 113:236–244

  • Katoh S, San Pietro A (1966) Activities of chloroplast fragments: I. Hill reaction and ascorbate-indophenol photoreduction. J Biol Chem 241:3575–3581

  • Shavit N, San Pietro A (1967) K+-Dependent uncoupling of photophosphorylation by nigericin. Biochem Biophys Res Commun 28:277–283

  • Gross E, Shavit N, San Pietro A (1968) An inhibitor of energy transfer in chloroplasts. Arch Biochem Biophys 127:224–228

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

Appendix 3

Examples of some publications from Indiana University (arranged chronologically) are:

  • Yocum CF, San Pietro A (1969) Ferredoxin reducing substance from spinach Biochem Biophys Res Commun 36:614–620

  • Klemme B, Klemme JH, San Pietro A (1971) PPase, ATPase and photophosphorylation in chromatophores of Rhodospirillum rubrum: Inactivation by phospholipase and reconstitution by phospholipids. Arch Biochem Biophys 144: 339–342

  • Brand J, San Pietro A, Mayne BC (1972) Site of polylysine inhibition of photosystem I in spinach chloroplasts. Arch Biochem Biophys 152:426–428

  • Siedow JN, Curtis VA, San Pietro A (1973) Studies on Photosystem I: 1 Relationship of plastocyanin, Cytochrome f and P700. Arch Biochem Biophys 158:889–897

  • Siedow JN, Yocum, CF, San Pietro A (1973) The reducing side of photosystem I. In: Sanadi DR, Packer L (eds) Current Topics in Bioenergetics, pp 107–123, Academic Press, NY

  • Lien S, San Pietro A (1975) An inquiry into biophotolysis of water to produce hydrogen. pp 1–50, Publication Prepared for US NSF (National Science Foundation)

  • Golbeck JH, Lien S, San Pietro A (1976) Quantitation of labile sulfide content and P700 photochemistry in spinach photosystem I particles. Biochem Biophys Res Commun 71:452–458

  • Davis DJ, San Pietro A (1977) Chemical modification of ferredoxin: evidence for a complex between ferredoxin and ferredoxin-NADP oxidoreductase in NADP photoreduction. Biochem Biophys Res Commun 74:33–40

  • McBride, AC, Lien S, Togasaki RK, San Pietro A (1977) Mutational analysis of Chlamydomonas reinhardi in chloroplast membranes: Application to biological solar energy conversion. In: Mitsui A, Miyachi S, San Pietro A, Tamura S (eds) Biological Solar Energy Conversion, pp 77–86, Academic Press, New York

  • Shavit N, Lien S, San Pietro A (1977) On the role of membrane-bound ADP and ATP in photophosphorylation in chloroplast membranes. FEBS Letters 73:55–58

  • Bookjans G, San Pietro A, Boger P (1978) Resolution and reconstitution of spinach ferredoxin-NADP oxidoreductase. Biochim Biophys Acta 80:759–765.

  • Lien S, San Pietro A. (1981) Effect of uncouplers on anaerobic adaptation hydrogenase activity in C. reinhardtii. Biochem Biophys Res Commun 103:139–147

  • Sakurai H, San Pietro A (1985) Association of Fe-S center(s) with the large subunits of photosystem I particles. J Biochem (Japan) 98:69–76

Rights and permissions

Reprints and permissions

About this article

Cite this article

San Pietro, A. Memories: from protein synthesis to photosynthesis. Photosynth Res 96, 185–199 (2008). https://doi.org/10.1007/s11120-008-9298-x

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s11120-008-9298-x

Keywords

Search

Navigation