Photosynthesis Research

, Volume 129, Issue 2, pp 109–127 | Cite as

Gernot Renger (1937–2013): his life, Max-Volmer Laboratory, and photosynthesis research

  • Ulrich SiggelEmail author
  • Franz-Josef Schmitt
  • Johannes MessingerEmail author
History and Biography


Gernot Renger (October 23, 1937–January 12, 2013), one of the leading biophysicists in the field of photosynthesis research, studied and worked at the Max-Volmer-Institute (MVI) of the Technische Universität Berlin, Germany, for more than 50 years, and thus witnessed the rise and decline of photosynthesis research at this institute, which at its prime was one of the leading centers in this field. We present a tribute to Gernot Renger’s work and life in the context of the history of photosynthesis research of that period, with special focus on the MVI. Gernot will be remembered for his thought-provoking questions and his boundless enthusiasm for science.


Max-Volmer-Institute Horst T. Witt Photosystem II Oxygen evolving complex Water oxidizing complex (WOC) ADRY agent Mechanism of water splitting 



Acceleration of the deactivation reactions of the water splitting system Y


PS II  membrane fragments prepared according to the protocol developed by Berthold, Babcock and Yocum


Carbonyl cyanide m-chlorophenyl hydrazone

Chl a

Chlorophyll a


Primary electron donor Chl of PSII (= P680)

CP43, CP47

Inner chlorophyll-binding antenna proteins of PSII with molecular masses of 43 and 47 kDa, repectively

D1, D2

Reaction center proteins of PSII


Diuron = 3-(3′-4′-dichlorophenyl)-1,1-dimethylurea

FU Berlin

Freie Universität Berlin


German Democratic Republic

HU Berlin

Humboldt Universität Berlin


Light harvesting complex




Oxygen-evolving complex


Primary electron donor of PSII (= Chl a II)


Primary electron donor of photosystem I




Pheophytin (primary electron acceptor of PSII)




Photosystem II


Primary and secondary plastoquinone molecules in PSII


Reactive oxygen species


Sonderforschungsbereich (CRC, collaborative research center)


Oxidation states of the oxygen-evolving complex of PSII (i = 0, 1, 2, 3, 4)


Superoxide dismutase

TU Berlin

Technische Universität Berlin


Water-oxidizing complex, equivalent of OEC


Water-soluable chlorophyll-binding protein


World War II


An intermediate with an absorption change at 320 nm; an early expression for QA


Tyrosine D of the D2 protein that can reduce the S2 and S3 states of PSII


Tyrosine Z of the D1 protein of PSII that acts as primary electron donor to P680+



We thank Govindjee for his encoragement during writing of this tribute and for his many editorial suggestions, and Dmitriy Shevela for redrawing Figs. 2, 6 and 7. This manuscript was also read and commented by Rajni Govindjee, Wolfgang Junge, Charles Dismukes, Jian-Ren Shen, Vittal Yachandra and Robert Blankenship before its publication.


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Copyright information

© Springer Science+Business Media Dordrecht 2016

Authors and Affiliations

  1. 1.Max-Volmer-LaboratoriumTU BerlinBerlinGermany
  2. 2.Departmant of ChemistryUmeå UniversityUmeåSweden

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