Abstract
This article provides a glimpse into the dawning of research on chlorophyll–protein complexes and a brief recollection of the path that led us to the identification of the photosystem II reaction center, i.e., the polypeptides that carry the site of primary charge separation in oxygenic photosynthesis. A preliminary version of the personal review on the latter topic has already appeared in this journal (Satoh Photosynth Res 76:233–240, 2003).
Similar content being viewed by others
Abbreviations
- Chl:
-
Chlorophyll
- CP-43, CP-47:
-
Antennas of the PS II core complex
- D1, D2 proteins:
-
Reaction center subunits of the PS II
- EPR:
-
Electron paramagnetic resonance
- LHCP:
-
Light harvesting Chl a/b protein of the PS II
- P680, P700:
-
Primary electron donor of the PS II and PS I, respectively
- PS I, PS II:
-
Photosystem I and photosystem II, respectively
- QA, QB :
-
Primary and secondary plastoquinone acceptors, respectively
- PAGE:
-
Polyacrylamide gel electrophoresis
- YZ, YD :
-
Redox active tyrosine on D1 and D2 proteins, respectively
References
Alt J, Morris J, Westhoff P, Herrmann RG (1984) Nucleotide sequence of the clustered genes for the 44 kd chlorophyll a apoprotein and the “32 kd”-like protein of the photosystem II reaction center in the spinach plastid chromosome. Curr Genet 8:597–606. doi:10.1007/BF00395705
Barber J (1984) Has the mangano-protein of the water splitting reaction of photosynthesis been isolated? Trends Biochem Sci 9:79–80. doi:10.1016/0968-0004(84)90093-8
Barry BA, Babcock GT (1987) Tyrosine radicals are involved in the photosynthetic oxygen-evolving system. Proc Natl Acad Sci USA 84:7099–7103. doi:10.1073/pnas.84.20.7099
Berthold DA, Babcock GT, Yocum JF (1981) A highly resolved oxygen-evolving photosystem II preparation from spinach thylakoid membranes. FEBS Lett 134:231–234. doi:10.1016/0014-5793(81)80608-4
Boardman NK, Anderson JM (1964) Isolation from spinach chloroplasts of particles containing different proportions of chlorophyll a and chlorophyll b and their possible role in the light reactions of photosynthesis. Nature 293:166–167. doi:10.1038/203166a0
Bricker TM, Pakrasi HB, Sherman LA (1985) Characterization of a spinach photosystem II core preparation isolated by a simplified method. Arch Biochem Biophys 237:170–176. doi:10.1016/0003-9861(85)90266-8
Brown JS (1972) Forms of chlorophyll in vivo. Annu Rev Plant Physiol 23:73–86. doi:10.1146/annurev.pp.23.060172.000445
Butler WL, Strasser RJ (1977) Tripartite model for the photochemical apparatus of green plant photosynthesis. Proc Natl Acad Sci USA 74:3382–3385. doi:10.1073/pnas.74.8.3382
Camm EL, Green BR (1983) Relationship between the two minor chlorophyll a–protein complexes and the photosystem II reaction centre. Biochim Biophys Acta 724:291–293. doi:10.1016/0005-2728(83)90148-2
Chua N-H, Bennoun P (1975) Thylakoid membrane polypeptides of Chlamydomonas reinhardtii: wild-type and mutant strains deficient in photosystem II reaction center. Proc Natl Acad Sci USA 72:2175–2179. doi:10.1073/pnas.72.6.2175
Danielius RV, Satoh K, van Kan PJM, Plijter JJ, Nuijs AM, van Gorkom HJ (1987) The primary reaction of photosystem II in the D1–D2-cytochrome b559 complex. FEBS Lett 213:241–244. doi:10.1016/0014-5793(87)81498-9
de Vitry C, Wollmann F-A, Delepelaire P (1984) Function of polypeptides of photosystem II reaction center in Chlamydomonas reinharditti. Biochim Biophys Acta 767:415–422. doi:10.1016/0005-2728(84)90039-2
Debus RJ, Barry BA, Babcock GT, McIntosh L (1988a) Site-directed mutagenesis identifies a tyrosine radical involved in the photosynthetic oxygen evolving system. Proc Natl Acad Sci USA 85:427–430. doi:10.1073/pnas.85.2.427
Debus RJ, Barry BA, Sithole I, Babcock GT, McIntosh L (1988b) Directed mutagenesis identifies that the donor to P680 in photosystem II is Tyr-161 of the D1 polypeptide. Biochemistry 27:9071–9074. doi:10.1021/bi00426a001
Deisenhofer J, Epp O, Miki K, Huber R, Michel H (1985) Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3Å resolution. Nature 318:618–624. doi:10.1038/318618a0
Döring G, Bailey JL, Kreutz W, Witt HT (1968) The active chlorophyll-a II in light reaction II of photosynthesis. Naturwissenschaften 55:219–224. doi:10.1007/BF00606205
Duysens LNM, Amesz J, Kamp BM (1961) Two photochemical systems in photosynthesis. Nature 190:510–511. doi:10.1038/190510a0
Ellis RJ (1977) Protein synthesis by isolated chloroplasts. Biochim Biophys Acta 463:185–215
Emerson R, Arnold W (1932a) A separation of the reactions in photosynthesis by means of intermittent light. J Gen Physiol 15:391–420. doi:10.1085/jgp.15.4.391
Emerson R, Arnold W (1932b) The photochemical reaction in photosynthesis. J Gen Physiol 16:191–205. doi:10.1085/jgp.16.2.191
Engelmann TW (1882) Über Sauerstoffausscheidung von Pflanzenzellen im Mikrospectrum. Bot Z 40:419–426
Evans MCW (1987) Plant reaction centre defined. Nature 327:284–285. doi:10.1038/327284a0
Ferreira KN, Iverson TM, Maghlaoui K, Barber J, Iwata S (2004) Architecture of the photosynthetic oxygen-evolving center. Science 303:1831–1837. doi:10.1126/science.1093087
Fischer E (1906) Untersuchungen über Aminosäuren, Polypeptide und Proteine. Ber Dtsch Chem Ges 33:530–610. doi:10.1002/cber.19060390190
Fischer H, Stern A (1940) Die Chemie des pyrrols, vol 2, Part II. Akad Verlagsges, Lepzig
French CS (1938) The chromoproteins of photosynthetic purple bacteria. Science 88:60–62. doi:10.1126/science.88.2272.60
French CS (1971) The distribution and action in photosynthesis of several forms of chlorophyll. Proc Natl Acad Sci USA 68:2893–2897. doi:10.1073/pnas.68.11.2893
Gaffron H, Whol K (1936) Zur Theorie der Assimilation. Naturwissenschaften 24:81–90, 103–107. doi:10.1007/BF01473561
Gounaris K, Barber J (1985) Isolation and characterization of a photosystem II reaction center lipoprotein complex. FEBS Lett 188:68–72. doi:10.1016/0014-5793(85)80876-0
Hill R, Bendall F (1960) Function of the cytochrome components in chloroplasts: a working hypothesis. Nature 186:136–137. doi:10.1038/186136a0
Hofmeister F (1902) Über Bau und Gruppierung der Eiweiss-körper. Ergeb Physiol 1:759–802
Huzisige H, Usiyama H, Kikuti T, Azi T (1969) Purification and properties of the photoactive particle corresponding to photosystem II. Plant Cell Physiol 10:441–455
Ikeuchi M, Inoue Y (1988) A new 4.8-kDa polypeptide intrinsic to the PS II reaction center, as revealed by modified SDS-PAGE with improved resolution of low-molecular-weight proteins. Plant Cell Physiol 29:1233–1239
Ikeuchi M, Yuasa M, Inoue Y (1985) Simple and discrete isolation of an O2-evolving PS II reaction center complex retaining Mn and the extrinsic 33 kDa protein. FEBS Lett 185:316–322. doi:10.1016/0014-5793(85)80930-3
Kamiya N, Shen J-R (2003) Crystal structure of oxygen-evolving photosystem II from Thermosynechococcus vulcanus at 3.7-Å resolution. Proc Natl Acad Sci USA 100:98–103. doi:10.1073/pnas.0135651100
Kashino Y, Lauber WM, Carroll JA, Wang Q, Whitmarsh J, Satoh K, Pakrasi HB (2002) Proteomic analysis of a highly active photosystem II preparation from the Synechocystis sp. PCC 6803 reveals the presence of novel polypeptides. Biochemistry 41:8004–8012. doi:10.1021/bi026012+
Kato Y, Nakamura K, Hashimoto T (1982) Evaluation of conventional and medium-performance anion exchangers for the separation of proteins. J Chromatogr 253:219–225. doi:10.1016/S0021-9673(01)88379-5
Kendrew JC, Dickerson RE, Strandberg BE, Hart RG, Davies DR, Phillips DC et al (1960) Structure of myoglobin: a three-dimensional Fourier synthesis at 2 Å resolution. Nature 185:422–427. doi:10.1038/185422a0
Klein SM, Vernon LP (1974) Protein composition of spinach chloroplasts and their photosystem I and photosystem II subfragments. Photochem Photobiol 19:43–49. doi:10.1111/j.1751-1097.1974.tb06472.x
Klimov VV, Klevanik AV, Shuvalov VA, Krasnowsky AA (1977) Reduction of pheophytin in the primary light reaction of photosystem II. FEBS Lett 82:183–186. doi:10.1016/0014-5793(77)80580-2
Kobayashi M, Maeda H, Watanabe T, Nakane H, Satoh K (1990) Chlorophyll a and β-carotene content in the D1/D2/cytochrome b-559 reaction center complex from spinach. FEBS Lett 260:138–140. doi:10.1016/0014-5793(90)80086-X
Koike H, Inoue Y (1983) Preparation of oxygen-evolving photosystem II particles from a thermophilic blue-green alga. In: Inoue Y, Crofts AR, Govindjee , Murata N, Renger G, Satoh K (eds) Oxygen evolving system of photosynthesis. Academic Press, Tokyo, pp 257–263
Kupke DW, French CS (1961) Relationship of chlorophyll to protein and lipids: molecular and colloidal solutions. Chlorophyll units. In: Ruhland W (ed) Encycl plant physiol, vol V (1). Springer-Verlag, Berlin, pp 298–322
Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–685. doi:10.1038/227680a0
Loll B, Kern J, Saenger W, Zouni A, Biesiadka J (2005) Towards complete cofactor arrangement in the 3.0 Å resolution structure of photosystem II. Nature 438:1040–1044. doi:10.1038/nature04224
Lubimenko V (1927) Reserches sur les pigments des plastes et sur la photosynthesis. I. Les pigments des plastes et leur transformation dans les tissues vivants de la plante. 1. Les pigments des chloroplasts. Rev Gen Bot 39:547–559
Malcolm DB (1978) The decline and fall of protein chemistry? Nature 275:90–91. doi:10.1038/275090a0
Mestre H (1930) The investigation of the pigments of the living photosynthetic cell. In: Contributions to marine biology. Stanford University Press, Stanford, pp 170–187
Michel H, Deisenhofer J (1985) X-ray diffraction studies on cryatalline bacterial photosynthetic reaction center: a progress report and conclusions on the structure of photosystem II reaction centers. In: Staehelin LA, Arntzen CJ (eds) Encyclopedia of plant physiology; new series photosynthesis, vol III. Springer-Verlag, Berlin, pp 371–381
Morris J, Hermann RG (1984) Nucleotide sequence of the gene for the P680 chlorophyll a apoprotein of the photosystem II reaction center from spinach. Nucleic Acids Res 12:2837–2850. doi:10.1093/nar/12.6.2837
Nakatani HY, Ke B, Dolan E, Arntzen CJ (1984) Identity of the photosystem II reaction center polypeptide. Biochim Biophys Acta 765:347–352. doi:10.1016/0005-2728(84)90175-0
Nanba O, Satoh K (1987) Isolation of a photosystem II reaction center consisting of D-1 and D-2 polypeptides and cytochrome b-559. Proc Natl Acad Sci USA 84:109–112. doi:10.1073/pnas.84.1.109
Ogawa T, Obata F, Shibata K (1966) Two pigment proteins in spinach chloroplasts. Biochim Biophys Acta 112:223–234. doi:10.1016/0926-6585(66)90323-2
Ohyama K, Fukuzawa H, Kohchi T, Shirai H, Sano S, Umesono K et al (1986) Chloroplast gene organization deduced from complete sequence of liverwort Marchantia polymorpha chloroplast DNA. Nature 322:572–574. doi:10.1038/322572a0
Okamura MY (1984) On the herbicide site in bacterial reaction centers. In: Thornber JP, Staehelin LA, Hallick PR (eds) Biosynthesis of the photosynthetic apparatus: molecular biology, development and regulation. Alan R Liss, Inc, New York, pp 381–390
Okamura MY, Satoh K, Issacson RA, Feher G (1987) Evidence of the primary charge separation in the D1/D2 complex of photosystem II from spinach: EPR of the triplet state. In: Biggins J (ed) Progress in photosynthesis research, vol 1. Martinus Nijhoff, Boston, pp 379–381
Pelletier PJ, Caventou JB (1818) Sur la matiere verte des feuilles. Ann Chim Phys Ser II 9:194–196
Perutz MF, Rossmann MG, Cullis AF, Muirhead H, Will G, North ACT (1960) Structure of haemoglobin: a three-dimensional Fourier synthesis at 5.5-Å resolution, obtained by X-ray analysis. Nature 185:416–422. doi:10.1038/185416a0
Pfister K, Steinback KE, Gardner G, Arntzen CJ (1981) Photoaffinity labeling of an herbicide receptor protein in chloroplast membranes. Proc Natl Acad Sci USA 78:981–985. doi:10.1073/pnas.78.2.981
Priestley J (1772) Observations on different kinds of air. Philos Trans R Soc Lond 62:147–264
Rabinowitch EI (1945) Photosynthesis and related processes, vol I. Wiley (Interscience), New York, pp 1–599
Racker F (1984) Resolution and reconstitution of biological pathways from 1919 to 1984. Fed Proc 42:2899–2909
Rochaix J-D, Dron M, Rahire M, Malone P (1984) Sequence homology between the 32 K dalton and the D2 chloroplast membrane polypeptides of Chlamydomonas reinhardtii. Plant Mol Biol 3:363–370. doi:10.1007/BF00033383
Sanger F (1952) The arrangement of amino acids in proteins. Adv Protein Chem 7:1–69. doi:10.1016/S0065-3233(08)60017-0
Sapozhnikov DI, Maslova TG (1956) The state of chlorophyll in leaves of green plants. Trans Bot Inst A H SSSR Ser IV 11:97–115 (Russian)
Satoh K (1979) Polypeptide composition of the purified photosystem II pigment-protein complex from spinach. Biochim Biophys Acta 546:84–92. doi:10.1016/0005-2728(79)90172-5
Satoh K (1980) F-695 emission from the purified photosystem II chlorophyll a–protein complex. FEBS Lett 110:53–56. doi:10.1016/0014-5793(80)80021-4
Satoh K (1982) Fractionation of thylakoid-bound chlorophyll-protein complexes by isoelectric focusing. In: Edelman M, Hallick RB, Chua N-H (eds) Methods in chloroplast molecular biology. Elsevier Biomed Press, Amsterdam, pp 845–856
Satoh K (1983) Photosystem II reaction center complex purified from higher plants. In: Inoue Y, Crofts AR, Govindjee , Murata N, Renger G, Satoh K (eds) Oxygen evolving system of photosynthesis. Academic Press, Tokyo, pp 27–38
Satoh K (1985) Protein-pigments and photosystem II reaction center. Photochem Photobiol 42:845–853. doi:10.1111/j.1751-1097.1985.tb01656.x
Satoh K (1986) Photosystem II particles largely depleted in the two intrinsic polypeptides in the 30 kDa region from Synechococcus sp.: identification of a subunit which carries the photosystem II reaction center. FEBS Lett 204:357–362. doi:10.1016/0014-5793(86)80843-2
Satoh K (1988) Reality of P-680 chlorophyll protein-Identification of the site of primary photochemistry in oxygenic photosynthesis. Physiol Plant 72:209–212. doi:10.1111/j.1399-3054.1988.tb06645.x
Satoh K (2003) The identification of the photosystem II reaction center: a personal story. Photosynth Res 76:233–240. doi:10.1023/A:1024933610778
Satoh K, Butler WL (1978) Low temperature spectral properties of subchloroplast fractions purified from spinach. Plant Physiol 61:373–379
Satoh K, Katoh S (1985) Inhibition by ethylenediamine tetraacetate and restoration by Mn2+ and Ca2+ of oxygen-evolving activity in photosystem II preparation from the thermophilic cyanobacterium, Synechococcus sp. Biochim Biophys Acta 806:221–229. doi:10.1016/0005-2728(85)90099-4
Satoh K, Yamamoto Y (2007) The carboxyl-terminal processing of precursor D1 protein of the photosystem II reaction center. Photosynth Res 94:203–215. doi:10.1007/s11120-007-9191-z
Satoh K, Nakatani HY, Steinback KE, Watson J, Arntzen CJ (1983) Polypeptide composition of a photosystem II core complex: presence of a herbicide-binding protein. Biochim Biophys Acta 724:142–150. doi:10.1016/0005-2728(83)90035-X
Satoh K, Fujii Y, Aoshima T, Tado T (1987) Immunological identification of the polypeptide bands in the SDS-polyacrylamide gel electrophoresis of photosystem II preparations. FEBS Lett 216:7–10. doi:10.1016/0014-5793(87)80746-9
Shen J-R, Inoue Y (1993) Binding and functional properties of two new extrinsic components, cytochrome c-550 and a 12 kDa protein, in cyanobacterial photosystem II. Biochemistry 32:1825–1832. doi:10.1021/bi00058a017
Shen J-R, Ikeuchi M, Inoue Y (1992) Stoichiometric association of extrinsic c-550 and 12 kDa protein with a purified oxygen-evolving photosystem II core complex from Synechococcus vulcanus. FEBS Lett 301:145–149. doi:10.1016/0014-5793(92)81235-E
Shibata K (1931) Carbon and nitrogen assimilation. Iwanami Shoten, Tokyo (Japanese) (English trans: Gest H, Togasaki RK (1975) Japan Science Press, Tokyo)
Shinozaki K, Ohme M, Tanaka M, Wakasugi T, Hayashida N, Matsubayashi T et al (1986) The complete nucleotide sequence of the tobacco chloroplast genome: its gene organization and expression. EMBO J 5:2043–2049
Smith EL (1938) Solution of chlorophyll-protein compounds (phyllochlorins) extracted from spinach. Science 88:170–172. doi:10.1126/science.88.2277.170
Smith EL (1941) The chlorophyll-protein compound of the green leaf. J Gen Physiol 24:565–582. doi:10.1085/jgp.24.5.565
Smith JHC (1952) Factor affecting the transformation of protochlorophyll to chlorophyll. Carnegie Inst Wash Year Book 51:151–153
Stoll A (1936) Zusammenhänge zwischen der Chemie des Chlorophylls und seiner Funktion in der Photosynthese. Naturwissenschaften 24:53–59. doi:10.1007/BF01473802
Sumner JB (1926) The isolation and crystallization of the enzyme urease. Preliminary paper. J Biol Chem 69:435–441
Takahashi Y, Takahashi M, Satoh K (1986) Identification of the site of iodide photooxidation in the photosystem II reaction center complex. FEBS Lett 208:347–351. doi:10.1016/0014-5793(86)81047-X
Takahashi Y, Hansson Ö, Mathis P, Satoh K (1987) Primary radical pair in the photosystem II reaction center. Biochim Biophys Acta 893:49–59. doi:10.1016/0005-2728(87)90147-2
Tang X-S, Satoh K (1984) Characterization of a 47-kilodalton chlorophyll-binding polypeptide (CP-47) isolated from a photosystem II core complex. Plant Cell Physiol 25:935–945
Tang X-S, Satoh K (1985) The oxygen-evolving photosystem II core complex. FEBS Lett 179:60–64. doi:10.1016/0014-5793(85)80191-5
Thomas JB, Blaauw OH, Duysens LNM (1953) On the relation between size and photochemical activity of fragments of spinach grana. Biochim Biophys Acta 10:230–240. doi:10.1016/0006-3002(53)90247-9
Thornber JP, Highkin HR (1974) Composition of the photosynthetic apparatus of normal barley leaves and a mutant lacking chlorophyll b. Eur J Biochem 41:109–116. doi:10.1111/j.1432-1033.1974.tb03250.x
Thornber JP, Smith CA, Bailey JL (1966) Partial characterization of two chlorophyll-protein complexes isolated from spinach-beet chloroplasts. Biochem J 100:14p–15p
Thornber JP, Markwell JP, Reinman S (1979) Plant chlorophyll–protein complexes: recent advances. Photochem Photobiol 29:1205–1216. doi:10.1111/j.1751-1097.1979.tb07840.x
Thornton LE, Roose JL, Pakrasi HB, Ikeuchi M (2005) The low molecular weight proteins of photosystem II. In: Wydrzynski TJ, Satoh K (eds) Photosystem II: the light-driven water:plastoquinone oxidoreductase. Springer, Dordrecht, pp 121–138
Trebst A (1986) The topology of the plastoquinone and herbicide binding peptides of photosystem II in the thlakoid membrane. Z Naturforsch 41c:240–245
Tswett MS (1901) Chlorophyllous grains. Travaux Soc Kazan 35:1–268 (Russian)
Vernon LP, Shaw ER, Ogawa T, Raveed D (1971) Structure of photosystem I and photosystem II of plant chloroplasts. Photochem Photobiol 14:343–357. doi:10.1111/j.1751-1097.1971.tb06178.x
Wassink EC (1948) Some remarks on chromophyllin and the paths of energy transfer in photosynthesis. Enzymologia 12:362–372
Wessels JSC (1962) Separation of the two photochemical systems of photosynthesis by digitonin fragmentation of spinach chloroplasts. Biochim Biophys Acta 65:561–564. doi:10.1016/0006-3002(62)90476-6
Wessels JSC, van Alphen-van Waveren O, Voorn G (1973) Isolation and properties of particles containing the reaction center complex of photosystem II from spinach chloroplasts. Biochim Biophys Acta 292:741–752. doi:10.1016/0005-2728(73)90021-2
Westhoff P, Alt J, Herrmann RG (1983) Localization of the genes for the two chlorophyll a-conjugated polypeptides (mol. wt. 51 and 44 kd) of the photosystem II reaction center on the spinach plastid chromosome. EMBO J 2:2229–2237
Willstätter R, Stoll A (1913) Untersuchungen über Chlorophyll. Justus Springer, Berlin (English trans: Schertz FM, Merz AR (1928) Science Printing Press, Lancaster, PA)
Witt HT (2005) Photosystem II: structural elements, the first 3D crystal structure and functional implications. In: Wydrzynski TJ, Satoh K (eds) Photosystem II: the light-driven water:plastoquinone oxidoreductase. Springer, Dordrecht, pp 425–447
Woodward RB, Ayer WA, Beaton JM, Bickelhaupt F, Bonnett R, Buchschacher P et al (1960) The total synthesis of chlorophyll. J Am Chem Soc 82:3800–3802. doi:10.1021/ja01499a093
Wydrzynski TJ, Satoh K (2005) Photosystem II: the light-driven water:plastoquinone oxidoreductase. Springer, Dordrecht
Yamada Y, Itoh N, Satoh K (1985) A versatile chromatographic procedure for purifying PS II reaction center complex from digitonin extracts of spinach thylakoids. Plant Cell Physiol 26:1263–1271
Yamagishi A, Katoh S (1983) Two chlorophyll-binding subunits of the photosystem II reaction center complex from the thermophilic cyanobacterium Synechoccoccus sp. Arch Biochem Biophys 225:836–846. doi:10.1016/0003-9861(83)90096-6
Yamagishi A, Katoh S (1984) A photoactive photosystem II reaction-center complex lacking a chlorophyll-binding 40 kilodalton subunit from the thermophilic cyanobacterium Synechoccoccus sp. Biochim Biophys Acta 765:118–124. doi:10.1016/0005-2728(84)90004-5
Yamaoka T, Satoh K, Katoh S (1978) Photosynthetic activities of a thermophilic blue-green alga. Plant Cell Physiol 19:943–954
Zouni A, Witt HT, Kern J, Fromme P, Krauss N, Saenger W et al (2001) Crystal structure of photosystem II from Synechococcus elongatus at 3.8 Å resolution. Nature 409:739–743. doi:10.1038/35055589
Zurawski G, Bohnert HJ, Whitfeld PR, Bottomley W (1982) Nucleotide sequence of the gene for the Mr 32, 000 thylakoid membrane protein from Spinacia oleracea and Nicotiana debneyi predicts a totally conserved primary translation product of Mr 38, 950. Proc Natl Acad Sci USA 79:7699–7703. doi:10.1073/pnas.79.24.7699
Acknowledgments
The author is grateful to the late Hirosi Huzisige for his guidance during the early part of my research career, to the students and colleagues in Okayama University, especially to Xiao-Song Tang, Yoshiaki Yamada, Osamu Nanba, and Yuichiro Takahashi, for their contribution to the progress in this line of research, and to the late Warren Butler, Paul Mathis, Charles Arntzen, George Feher, Melvin Okamura, Hans van Gorkom, and the late Arnold Hoff for their collaborations and encouragements. The author would like to express thanks to the editors of this special issue for inviting to write the article, and Jian-Ren Shen and Isao Enami for their valuable discussion and help in preparing this manuscript.
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
About this article
Cite this article
Satoh, K. Protein-pigments and the photosystem II reaction center: a glimpse into the history of research and reminiscences. Photosynth Res 98, 33–42 (2008). https://doi.org/10.1007/s11120-008-9348-4
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s11120-008-9348-4