Rudolf K. Thauer

Rudolf K. Thauer
Emeritus Group
Rudolf K. Thauer
(Prof. Dr. Dr. h. c. mult)
born 05.10.1939
Study of Medicine (Frankfurt) and Biochemistry (Tübingen)
Dr. rer. Nat (Biochemistry), Freiburg, 1968
Habilitation (Biochemistry), Freiburg, 1971
Postdoc, Case Western Reserve, Cleveland, Ohio, 1972
Associate Professor of Biochemistry, Bochum, 1972-1976
Professor of Microbiology, Marburg, 1978-2005
Director at the MPI Marburg, 1991-2007
Emeritus at the MPI Marburg, since 11/2007
Leibniz Prize of the DFG, 1987
Biochemistry of methanogenic archaea:
Present and future projects
In the last two years (2008 and 2009) my group continued or started to work on the following five interrelated
projects:
(i) The structure and function of [Fe]-hydrogenase, an
enzyme substituting for F420-reducing [NiFe]-hydrogenase in methanogenic archaea under conditions of nickel limitation, and the biosynthesis of its iron-containing
cofactor (Dr. Seigo Shima with Dr. Takeshi Hiromoto,
Michael Schick and Stella Vitt in collaboration with PD
Dr. Ulrich Ermler, MPI für Biophysik, Frankfurt).
(v) The construction of a Methanosarcina strain that can
grow on glucose forming 3 CO2 and CH4 (R. Thauer
with Christian Sattler in collaboration with Prof. Dr. Michael Rother, University Frankfurt).
(i) Structure, function and biosynthesis of [Fe]hydrogenase
There are three enzymes known to date that can reversibly activate H2, namely [NiFe]-hydrogenases, [FeFe]hydrogenases and [Fe]-hydrogenase (Fig. 1).
(ii) The catalytic mechanism of methyl-coenzyme M reductase catalyzing the methane forming step in methanogenic archaea and the oxidation of methane in methanotrophic archaea (R. Thauer with Dr. Meike Brefort
(Goenrich), Reinhard Böcher and Dr. Seigo Shima in
collaboration with Prof. Dr. Bernhard Jaun from the
ETH Zürich and Prof. Dr. Friedrich Widdel from the
MPI für marine Mikrobiologie in Bremen).
(iii) Mechanism of the enzyme complex catalyzing the
coupled reduction of ferredoxin and of the heterodisulfide CoM-S-S-CoB with H2 (R. Thauer with Anne
Kaster and Kristian Parey in collaboration with PD Dr.
Ulrich Ermler, MPI für Biophysik, Frankfurt).
(iv) Characterization of the enzyme system catalyzing
the coupled reduction of ferredoxin and NAD+ with
NADPH in Clostridium kluyveri (R. Thauer with Dr.
Shuning Wang, Johanna Moll und Haiyan Huang).
104
Fig. 1. The metal sites of the three types of hydrogenases. They
have unusual structural features in common such as intrinsic
CO ligands. Despite this fact [NiFe]-hydrogenase, [FeFe]-hydrogenases and [Fe]-hydrogenases are phylogenetically not
related, neither at the level of apoenzyme primary structure nor
at the level of the enzymes involved in their active site biosynthesis. -GMP, guanylyl rest.
These enzymes do this at much lower activation energies than e.g. platinum. Their catalytic mechanism is
therefore of considerably applied interest. Of the three
hydrogenases, the [Fe]-hydrogenase is unique in containing a mononuclear rather than a dinuclear metal
Rudolf K. Thauer
center and in lacking an iron-sulfur cluster (Shima et al.
2009). The iron in [Fe]-hydrogenase is associated with
an extractable organic cofactor covalently linked to the
protein only via one Fe-S-Cys bond (Fig. 1)
Upon denaturation of the enzyme in the presence of
mercaptoethanol [Fe]-hydrogenase can be reversibly
dissociated into apoenzyme and the iron guanylylpyridinol cofactor (FeGP-cofactor), the cysteine residue being
replaced by mercaptoethanol. Within the last years the
structures of the apoenzyme, holoenzyme and holoenzyme substrate complex have been elucidated (Shima et
al. 2008; Hiromoto et al. 2009 a and b, Salomone-Stagni
et al. 2010).
A comparison with [NiFe]-hydrogenases and [FeFe]-hydrogenases reveals striking structural similarities in the
active site structure (Fig. 1). Thus the three types of hydrogenases, two of which were discovered in Marburg,
contain in their active site a low spin iron with intrinsic
CO and cyanide ligands (in the case of [Fe]-hydrogenase the unique acyl-ligand to iron can be considered
as cyanide equivalent). For future studies of the catalytic mechanism our recent discovery is of importance
that some isocyanides can inhibit [Fe]-hydrogenase by
reversibly binding to the low spin iron with Ki lower than
0.1 µM (S. Shima, unpublished results).
We have initiated 13C-labeling studies indicating that of
the nine carbon of the pyridinol moiety of the FeGPcofactor three are derived from C1 of acetate, two from
C2 of acetate, one from the methyl group of methionine
and three from CO2 or the carboxyl group of pyruvate.
Via 1H and 13C NMR the labeling pattern will be determined. In parallel we have identified a gene cluster
most likely coding for FeGP-cofactor biosynthesis. Experiments have been initiated to heterologously express
these genes individually and together in Escherichia coli.
Also, mutational analyses of the biosynthesis genes in
Methanococcus maripaludis have been started in collaboration with Prof. Dr. Michel Rother, Universität
Frankfurt. The fact is exploited that [Fe]-hydrogenase
is required in methanogenic archaea only under conditions of nickel-limiting growth conditions (Thauer et al.
2010).
For a more detailed description of the results obtained
for [Fe]-hydrogenase see the chapter “Seigo Shima”.
Emeritus Group
(ii) The catalytic mechanism of methyl-coenzyme
M reductase
Methyl-coenzyme M reductase (MCR) catalyzes the
methane forming step in methanogenic archaea. The
enzyme has recently been proposed to be involved also
in the anaerobic oxidation of methane (AOM) with sulfate mediated by consortia of methanotrophic archaea
and sulfate-reducing delta-proteobacteria (Thauer and
Shima 2008; Ettwig et al. 2008; Jaun and Thauer 2009;
Fig. 2).
Fig. 2. Reaction catalyzed by the nickel enzyme methyl-coenzyme M reductase. The nickel in the enzyme is associated with
coenzyme F430, a corphinoid tetrapyrrole found unitl now only in
methanogenic archaea and methanotrophic archaea. The transition metal has to be in the Ni(I) oxidation state for the enzyme
to be active (Thauer et al. 2008; Jaun and Thauer 2009; Mayr et
al. 2008). 1 U = 1 µmol per min at 60 °C.
With respect to the catalytic mechanism our recent finding is of interest that upon reaction of MCR with its
coenzymes M and B a nickel hydride complex is formed
(Harmer et al. 2008). Nickel hydrides have been shown
to activate methane. Of importance is also our finding
that binding of coenzyme B induces a major conformational change in the active site of MCR most probably
leading to an increased nucleophilicity of the Ni(I) in
F430 (Ebner et al. 2009).
Using a novel NMR spectroscopic method, we were
able to show for the first time that MCR can catalyze
the back reaction at kinetics (apparent Km and Vmax)
consistent with the in vivo kinetics of AOM with sulfate
(Scheller et al. 2010). The crystal structure of MCR purified from mats catalyzing AOM revealed the presence
of coenzyme M and coenzyme B indicating that the enzyme uses the same coenzymes as MCR from methanogenic archaea (Shima et al. unpublished results). MCR
from methanotrophic archaea of the ANME-1 cluster
105
Emeritus Group
contain a modified F430, the structure of which was elucidated (Mayr et al. 2008).
Our findings of a NMR spectroscopic method allowing to follow the formation of methyl-coenzyme M from
methane and CoM-S-S-CoB opened the window to a
large number of experiments previously thought out of
reach. E. g. we have already shown using the method
that 12CH3-13CH2-S-CoM rapidly yields 13CH3-12CH2S-CoM upon incubation with MCR in the presence
coenzyme B. Ethyl-coenzyme M is reduced to ethane
by MCR albeit at a 200 fold lower catalytic efficiency
than methyl-coenzyme M is reduced to methane. The
mechanisms proposed so far for MCR cannot explain
this finding and must therefore be revised.
Fig. 3. Cartoon of the MvhADG- HdrABC complex highlighting
the putative functions of the individual subunits. The enzyme
complex couples the endergonic reduction of ferredoxin with
H2 to the exergonic reduction of CoM-S-S-CoB with H2 via the
mechanism of flavin-based electron bifurcation. n, mol Fdox
reduced per 2 mol H2, is not yet known. The redox potentials
are standard potentials at pH 7 (E°’). E°’ of this ferredoxin is
assumed to be -500 mV, which is the E°’ of the CO2/CHO-MFR
couple, the first step in CO2 reduction to methane. Abbreviations
used: Fd, ferredoxin; HS-CoM, coenzyme M; HS-CoB, coenzyme
B. The zinc in HdrB is ligated by 3 sulfur and a histidine nitrogen
as revealed by Zn K-edge X-ray absorption spectroscopy. The
four “C” in HdrA is a conserved sequence motif with 4 cysteines.
In HdrA from Methanococcus species one the four cysteines is a
selenocysteine.
(iii) Mechanism of the enzyme complex catalyzing
the coupled reduction of ferredoxin and of CoM-SS-CoB with H2
Two years ago we have proposed that the cytoplasmic
MvhADG/HdrABC complex from methanogenic archaea couples two reactions via a flavin-based electron
bifurcation, namely the endergonic reduction of ferredoxin with H2 to the exergonic reduction of the heterodisulfide (CoM-S-S-CoB) with H2 (Thauer et al. 2008).
106
Rudolf K. Thauer
In the meantime we could show that the purified enzyme complex catalyzes a CoM-S-S-CoB dependent
reduction of ferredoxin with H2. The stoichiometry of
coupling is not clear yet because the coupling in the purified complex is apparently not tight. The conditions of
tight coupling remain to be found.
In parallel to the coupling studies we are trying to crystallize the MvhADG/HdrABC complex and - after dissociation of the complex in the presence of detergents
- the hydrogenase subcomplex MvhADG and the heterodisulfide reductase subcomplex HdrABC. From the
crystal structure(s) it is hoped to get insight into the
mechanism of flavin-based electron bifurcation.
(iv) An enzyme system catalyzing the coupled
reduction of ferredoxin and NAD+ with NADPH in
Clostridium kluyveri
We have recently shown that in Clostridium kluyveri
the exergonic reduction of crotonyl-CoA with NADH
is coupled with the endergonic reduction of ferredoxin
with NADH via flavin-based electron bifurcation (Li et
al. 2008). This novel coupling mechanism allowed for
the first time to formulate a metabolic scheme for the
ethanol-acetate fermentation that could account for the
observed fermentation products and growth yields, and
thus for the observed ATP gains (Seedorf et al. 2008).
One question, however, remained open, namely, why the
formation of butyrate from ethanol and acetate in the
fermentation involves a NADP- and a NAD-specific ßhydroxybutyryl-CoA dehydrogenase despite the fact that
in the oxidative part of the fermentation only NADH is
generated. The presence of a reduced ferredoxin: NADP
oxidoreductase was proposed, which in the following we
looked for.
Cell extracts of C. kluyveri catalyze the NAD+-dependent reduction of ferredoxin with NADPH and the
reduction of NAD+ with NADPH. After partial purification and amino acid sequence determination of a
heterodimer, two neighboring genes were identified and
heterologously expressed in E. coli. The cell extracts of
the recombinant E. coli now also catalyzed the NAD+dependent reduction of ferredoxin with NADPH and
the transhydrogenation reaction. The activities were
shown to be FAD-dependent. From the available results
it appears that the heterologously produced enzyme
complex couples the exergonic reduction of NAD+ with
NADPH with the endergonic reduction of ferredoxin
with NADPH via flavin-based electron bifurcation. The
details of this reaction and of its catalyzing complex remain to be worked out.
Rudolf K. Thauer
(v) The construction of a Methanosarcina strain
that can grow on glucose
In anoxic environments cellulose, a polymer of glucose,
is fermented to CO2 and methane via a syntrophic association of anaerobic bacteria, protozoa and fungi that
ferment cellulose to acetic acid, CO2 and H2 and of
methanogenic archaea that convert acetic acid, CO2 and
H2 to methane. There is no organism known that can
ferment glucose to 3 CO2 and 3 CH4 alone. A kinetic
theory relating growth rates to the length of metabolic
pathways and the number of coupling sites can explain
these finding for energy substrate-limited planctonic
cells (Pfeiffer, T., Schuster, S. & Bonhoeffer,S. (2001)
Cooperation and Competition in the Evolution of ATPProducing Pathways. Science 292, 504-507). The same
theory predicts, however, that in biofilms methanogens
capable of fermenting glucose to CO2 and methane
should exist. To test this we want to clone the genes required for glucose-import and glucose activation to glucose-6-phosphate into Methanosarcina barkeri, a methanogen lacking only these genes for methanogenesis from
glucose for which a genetic system has been developed.
This project will be pursued together with Prof. Dr. Michael Rother from the University of Frankfurt who has
developed the genetic system. It is being financed by the
LOEWE center SYNMIKRO in Marburg.
Impact 2008-2009
Since start of the emeritus group on November 1, 2007,
the group submitted fifteen original papers of which end
of 2009 fourteen were published or were in press. The
results were additionally summarized in four reviews and
six book chapters. Many of the papers were published in
high impact journals such as Science, Angewandte Chemie, Journal of the American Chemical Society (JACS),
Proceedings of the National Academy of Sciences
(PNAS), Biochemistry, Journal of Bacteriology, Annals
of the New York Academy of Sciences, Nature Microbiology Reviews, and Annual Reviews of Biochemistry.
Until end of February 2010, the papers published since
2008 have already been cited more than 150 times.
In the group one student completed her doctoral thesis,
one his diploma thesis and one his bachelor thesis.
Emeritus Group
Publications
Original papers
Vogt, S., Lyon, E.J., Shima, S. and Thauer, R.K. (2008)
The exchange activities of [Fe] hydrogenase (iron-sulfurcluster-free hydrogenase) from methanogenic archaea in
comparison with the exchange activities of [FeFe] and
[NiFe] hydrogenases. J Biol Inorg Chem. 13, 97-106.
Guo, Y., Wang, H., Xiao, Y., Vogt, S., Thauer, R.K., Shima, S., Volkers, P.I., Rauchfuss, T.B., Pelmenschikov, V.,
Case, D. A., Alp, E., Sturhahn, W., Yoda, Y. & Cramer,
S.P. (2008) Characterization of the Fe site in iron-sulfur
cluster free hydrogenase (Hmd) and of a model compound via nuclear resonance vibrational spectroscopy
(NRVS). Inorganic Chemistry 47, 3969-3977.
Seedorf, H., Fricke, W.F., Veith, B., Brüggemann, H.,
Liesegang, H. Strittmatter, A., Miethke, M., Buckel, W.,
Hinderberger, J., Li, F., Hagemeier C.H., Thauer, R.K.
& Gottschalk, G. (2008) The genome of Clostridium
kluyveri, a strict anaerobe with unique metabolic features. Proc. Natl. Acad. Sci. 105, 2128-2133.
Li, F., Hinderberger, J., Seedorf, H., Zhang, J., Buckel,
W. & Thauer, R.K. (2008) Coupled ferredoxin and crotonyl coenzyme A (CoA) reduction with NADH catalyzed
by the butyryl-CoA dehydrogenasee/Etf complex from
Clostridium kluyveri. J. Bacteriol. 190, 843-850.
Ettwig, K.F., Shima, S., van de Pas-Schoonen, K.T.,
Kahnt, J., Medema, M., op den Camp, H.J.M. Jetten,
M.S.M. & Strous, M (2008) Denitrifying bacteria anaerobically oxidize methane in the absence of archaea.
Env. Microbiol. 10. 3164-3173.
Shima, S., Pilak O., Vogt, S., Schick, M., Stagni, M.S.,
Meyer-Klaucke, W., Warkentin, E., Thauer, R.K., &
Ermler, U.(2008) The crystal structure of [Fe]-hydrogenase reveals the geometry of the active site. Science
321, 572-575.
Harmer, J, Finazzo, C., Piskorski, R., Ebner, S., Duin,
E.C., Goenrich, M., Thauer, R.K., Reiher, M., Schweiger, A., Hinderberger, D. & Jaun, B (2008) A nickel hydride complex in the active site of methyl-coenzyme M
reductase: Implications for the catalytic cycle. J. Am.
Chem. Soc., 130, 10907-10920.
Mayr, S., Latkoczy C., Krüger, M., Günther, D., Shima,
S., Thauer, R.K., Widdel, F. & Jaun, B. (2008) Structure of an F430 variant from Archaea associated with an-
107
Rudolf K. Thauer
Emeritus Group
aerobic oxidation of methane. J. Am. Chem. Soc., 130,
10758-10767.
cally relevant differences in energy conservation. Nat.
Rev. Microbiol. 6, 579-591.
Hinderberger, D., Ebner, S., Mayr, S., Jaun, B., Reiher,
M., Goenrich, M., Thauer, R. K., & Harmer, J. (2008).
Coordination and binding geometry of methyl-coenzyme
M in the red1m state of methyl-coenzyme M reductase.
J. Biol. Inorg. Chem., 13, 1275-1289.
Thauer, R.K. Kaster, A.-K., Goenrich, M., Schick, M.,
Hiromoto, T. & Shima, S (2009) Hydrogenases from
methanogenic archaea, nickel, a novel cofactor and H2storage. Ann. Rev. Biochem., in press
Hiromoto, T., Ataka, K., Pilak O., Vogt, S., Stagni, M.S.,
Meyer-Klaucke, W., Warkentin, E., Thauer, R.K., Shima, S., & Ermler, U.(2009) The crystal structure of
C176A mutated [Fe]-hydrogenase suggests an acyl-iron
ligation in the active site iron complex. FEBS Letters
583, 585-590.
Hiromoto, T., Warkentin, E., Moll, J., Ermler, U., &
Shima, S. (2009) The crystal structure of an [Fe]-hydrogenase-Substrate complex reveals the framework for
H2 activation. Angew. Chem. Int. Ed. 48, 6457-6460.
Ceh, K., Demmer, U., Warkentin, E., Moll, J., Thauer,
R.K., Shima, S. & Ermler, U. (2009) Structural basis
of the hydride transfer mechanism in F420-dependent
methylenetetrahydromethanopterin
dehydrogenase.
Biochemistry 48, 10098-10105.
Salomone-Stagni, M., Stellato, F., Whaley, C.M., Vogt,
S., Morante, S., Shima, S., Rauchfuss, T.B., and MeyerKlaucke, W. (2010) The iron-site structure of [Fe]-hydrogenase and model systems: an X-ray absorption near
edge spectroscopy study. Dalton Trans., in press (DOI:
10.1039/b922557a).
Ebner, S., Jaun, B., Goenrich, M., Thauer, R. K. &
Harmer, J. (2010) Binding of coenzyme B induces a major conformational change in the active site of methylcoenzyme M reductase J. Am. Chem. Soc., in press
Scheller, S., Goenrich,M., Böcher R., Thauer R. K., &
Jaun, B. (2010) Reverse methanogenesis: the key nickel
enzyme MCR catalyses anaerobic oxidation of methane,
in revision.
Reviews in Journals
Thauer, R.K. & Shima, S. (2008) Methane as fuel for
anaerobic microorganisms. Ann. N. Y. Acad. Sci. 1125,
158-170.
Thauer, R. K., Kaster, A.K., Seedorf, H., Buckel, W., &
Hedderich, R. (2008) Methanogenic archaea: Ecologi-
108
Shima, S (2008) The structure of the [Fe]-hydrogenase
and the convergent evolution of the active site of hydrogenases. Seikagaku, 80, 846-849 (in Japanese).
Reviews in Books
Shima, S (2008) Functions of methyl-coenzyme M reductase in production and degradation of methane, pp.
182-183. In Applied Microbiology (Kumagai, H., Kato,
N., Murata, K. & Sakai, Y., eds) Asakura Shoten, Tokyo,
Japan (in Japanese).
Thauer, R.K. (2008) Of methanotrophic and Methanogenic Archaea. In: Life Strategies of Microorganisms in
the Environment and in Host Organisms (Amann R.,
Goebel, W., Reinhold-Hurek, B., Schink, B. and Widdel, F. eds. Nova Acta Leopoldina 96, 41-44.
Thauer, R.K. (2008) Biologische Methanbildung: Eine
erneuerbare Energiequelle von Bedeutung? In Die Zukunft der Energie (Gruss, P. und Schüth, Heraus-geber)
Verlag C. H. Beck, pp.119-137.
Friedrich, B. & Thauer, R.K. (2008) Molekularfunktion
von Katalysatoren bei der Produktion von BioH2. Jahrbuch 2007 der Deutschen Akademie der Naturforscher
Leopoldina, Wissenschaftliche Verlagsgesellschaft mbH
Stuttgart, pp. 349-350.
Jaun, B. & Thauer, R.K. (2009) Nickel-alkyl bond formation in the active site of methyl-coenzyme M reductase (MCR). In Metal-carbon bonds in enzymes and
cofactors, Vol.6 of Metal Ions in Life Sciences (Sigel, A.,
Sigel, H., Sigel, R.K.O., eds). John Wiley & Sons, Ltd,
Chichester, UK, pp. 115-132.
Shima, S., Thauer, R.K. & Ermler, U. (2009) Carbon
monoxide as intrinsic ligands to iron in the active site
of [Fe]-hydrogenase. In Metal-carbon bonds in enzymes
and cofactors, Vol. 6 of Metal Ions in Life Sciences (Sigel, A., Sigel, H., Sigel, R.K.O., eds). John Wiley & Sons,
Ltd, Chichester, UK, pp 219-240.
Rudolf K. Thauer
Emeritus Group
Miscellaneous
Structure of the group (12/2009)
Thauer, R.K. (2008) Leopoldina als nationale Akademie
der Wissenschaften. BIOspektrum 14, 567.
Group leader: Prof. Dr. Rudolf K. Thauer (emeritus)
ter Meulen, V. & Thauer, R.. (2009) Celebrating Achim
Trebst´s 80th birthday. Phoptosynthesis Research 100,
117-119.
Associated group leader: Seigo Shima, PhD (permanent position)
Secretary: Claudia Schäfer (1 hour per day)
Finished theses
PhD thesis
Hinderberger, Julia (2008) Ferredoxin Reduktion und
Oxidation im Stoff-wechsel von Clostridium kluyveri
Diploma thesis
Schick, Michael (2008) [Fe]-Hydrogenase (Hmd) in
zwei methanogenen Archaea ohne Gene für die vermuteten FeGP-Kofaktor Scaffold-Proteine Hmd II und
Hmd III.
BSc thesis
Daniel Andritschke (2008) Crotonyl-CoA: Acetat CoATransferase (Cat1) aus Clostridium kluyveri
Postdoctoral fellows: Dr. Meike Brefort (Goenrich)
(unil 10/10), Dr. Takeshi Hiromoto (until 08/10) and
Dr. Shuning Wang (until 10/10)
PhD students*): Anne Kaster (until 10/10), Kristian
Parey (until 10/10), Michael Schick (until 06/11), Stella Vitt (since 10/09), Christian Sattler (since 11/2009)
Technical assistants: Reinhard Böcher (50%) and
Johanna Moll (both permanent positions)
Research student: Huang Haiyan (since 03/09)
Guest Scientist: Alexander Netrusov (01/08, 07/08,
01/09, 07/09)
PhD thesis of Stella Vitt is being supervised together
with Dr. S. Shima and PD Dr. U. Ermler (MPI for
Biophysics Frankfurt). Michael Schick will be financed
via the PRESTO grant to S. Shima from April 2010.
The PhD thesis of Christian Sattler is being supervised
together with Prof. Dr. M. Rother (University of Frankfurt) and financed via the LOEWE grant to R. Thauer.
Written agreements have been made that Stella Vitt
and Christian Sattler will be able to finish their theses
and graduate in Frankfurt if this turns out to be necessary.
*)
External funding
Japan Science and Technology Agency (PRESTO Program): Euro 400 000 for 5 years starting 10/09 (to Seigo
Shima)
Fonds der Chemischen Industrie (to R. Thauer)
Memberships
Kuratorium der Angewandten Chemie
Präsidium der Deutsche Akademie der Naturforscher
Leopoldina: Nationale Akademie der Wissenschaften
Scientific Advisory Board of LanzaTech Limited, Auckland, New Zealand
Invited lectures abroad
Seminar, 16th April 2008, Inorganic Chemistry Laboratory, University of Oxford, United Kingdom.
Microbial Diversity Course, 21-29 June 2008, Woods
Hole, Massachusetts, USA (four lectures)
Fachbeirat Future Capital AG, Frankfurt
Fourth International Symposium on Biooranometallic
Chemistry, 16.-10 July, 2008, Missoula, Montana, USA
Gordon Research Conference on “Molecular Basis of
Microbial One-Carbon Metabolism, 20-25 July 2008,
Bates College, Lewiston, Maine, USA
109
Rudolf K. Thauer
Emeritus Group
XII. International Congress of Bacteriology and Applied
Microbiology, 5-9 August 2008, Istanbul, Turkey
Chinese Academy of Sciences (CAS) meeting, 10-14
November 2008, Peking, China
Bioenergy Genome Center, 17. November 2008,
Qingdao, China
EMBO-FEMS Workshop on Microbial Sulfur Metabolism, 15-18 March 2009, Tomar, Portugal
American Society for Microbiology 109th General Meeting, 17-21 May 2009, Philadelphia, Pennsylvania, USA
Gordon Research Conference on Archaea: Ecology, Metabolism and Molecular Biology, 26-31 July 2009, Waterville Valley, NH, USA
Gordon Research Conference on Vitamin B12 and Corphins, 2-7 August 2009, Oxford, United Kingdom
Seminar, 4th November 2009, Johannes Kepler Universität, Linz, Austria
Seminar, 11th November 2009, ETH Zürich, Switzerland
Awards
Carl Friedrich Gauß-Medaille, Braunschweigische Wissenschaftliche Gesellschaft 05/08
Honorary member of the „Vereinigung für Allgemeine
und Angewandte Mikrobiologie“ (VAAM) 03/09
110
Lab retreats
10.–15. August 2008 in Hirschegg, Kleinwalsertal, together with the group of Ulrich Ermler from the Max
Planck Institute for Biophysics in Frankfurt, the group
of Bernhard Jaun from the ETH Zürich, the Group of
Georg Fuchs from the University of Freiburg and the
groups of Wolfgang Buckel and Johann Heider from the
University of Marburg.
23.-28. August 2009 in Hirschegg, Kleinwalsertal, together with the group of Ulrich Ermler from the Max
Planck Institute for Biophysics in Frankfurt, the group
of Bernhard Jaun from the ETH Zürich, the group of
Georg Fuchs from the University of Freiburg and the
groups of Wolfgang Buckel and Johann Heider from the
University Marburg.
Address
Prof. Dr. Rudolf K. Thauer
Max-Planck-Institut für terrestrische Mikrobiologie
Karl-von-Frisch Straße 10
35043 Marburg/Germany
Phone: +49 6421 178-101
Fax: + 49 6421 178-109
E-mail: thauer@mpi-marburg.mpg.de
Rudolf K. Thauer
Emeritus Group
Seminar in Hirschegg, Kleinwalsertal, from 10.-15. August 2008.
First row (from left to right): Seigo
Shima; Johanna Moll; Anne-Kristin
Kaster; Sebastian Kölzer; Michael
Schick
Second row: Takeshi Hiromoto;
Astrid Brandis-Heep; Sieglinde
Ebner; Katharina Körner; Liv Rather;
Sibylle Ziegler
Third row: Georg Fuchs; Eberhard
Warkentin; A. Parthasrathy; Sylvan
Scheller; Ulrike Demmer; Berhard
Jaun; S. Marx; Kathrin Schneider;
M. Lippert; Rolf Thauer; Johann
Heider; Shuning Wang;
Last row: Reinhard Böcher; Ulrich
Ermler; Kristian Parey; Hana Pandelikova; D. Kockelhorn; A. Petri;
Robin Teufel, R.; D. Kathrei; Juri
Dermer; Michael Rother; Ivan Berg;
Karola. Schühle; Birgit Alber; T. Erb;
Hugo Ramos
Seminar in Hirschegg, Kleinwalsertal, from 23.-28. August 2009.
First row (from left to right): Tobias
Weinert; Meike Brefort; Anne-Kristin
Kaster; Ivan Berg; Seigo Shima
Second row: Michael Schick; Elamparithy Yamayayamani; Marie Kim;
Karola Schühle; Carlotta DebnarDaumler; Johann Heider; Takeshi
Hiromoto
Third row: Basem Soboh; Markus
Hilberg; Daniel Knack; Vikrant;
Sibylle Ziegler; Ulrike Demmer;
Anne Brettschneider; Hana Pandlikova; Michaela Voss; Liv Rather;
Astrid Brandis-Heep; Shuning
Wang; Johanna Moll.
Forth row: Rolf Thauer; Peter Friedrich; Eberhard Warkentin; Kristian Parey; Wolfgang Buckel; Janos Retey; Robin Teufel; Ulrich
Ermler; Constanze Pienske; Michael Cather; Frederick Lyatuu; Birgit Alber; Kathrin Schneider; Michael Rother
111