His research focuses on the elementary processes of photosynthesis and catalytic metal centers in
metalloproteins. He is an expert in the application of EPR spectroscopy and quantum chemical calculations. He has over 500 publications with more than 25,000 citations.[10]
EPR spectroscopy
Throughout his career, EPR has played an important role as a biophysical technique to gain information about radicals, radical pairs, triplet states and metal centers in chemistry and biochemistry.[1][11][5] Particular emphasis has been placed on methods that are able to resolve the electron-nuclear hyperfine couplings between the
electron spin and the
nuclear spins. Next to the more established techniques,
electron spin echo modulation (ESEEM) and
electron-nuclear double resonance (ENDOR), his group further developed and used electron-electron double resonance- (ELDOR) detected
NMR (EDNMR) at a range of mw frequencies.[12][13][14] These techniques have been used by him and his group to extensively study bacterial
photosynthetic reaction centres, their donor-acceptor model complexes,
photosystem I,
photosystem II,[1][5] and a number of different hydrogenases.[11][4]
Oxygen-evolving Complex
During his early career, bacterial
photosynthetic reaction centres and oxygenic
photosystem I and photosystem II[1] have been a main focus. He and his group studied light-induced
chlorophyll donor[2] and quinone acceptor radical ions[3] of the primary electron-transfer chain. Later his research focused on the
water splitting cycle (S-states) of
photosystem II using advanced multifrequency pulse EPR,
ENDOR and EDNMR techniques. His group was able to detect and characterize the flash-generated, freeze-trapped
paramagnetic states S0, S2 and S3 (S1 is diamagnetic and S4 is a transient state) of the Mn4Ca1Ox catalytic cluster. By a careful spectral analysis–backed up by
quantum chemical calculations the site
oxidation and
spin states of all
Mn ions and their spin coupling for all intermediates of the
catalytic cycle could be detected.[15][16][17] Further work using advanced Pulse EPR techniques, such as EDNMR, has led to information on the binding of water[18] and a proposal of an efficient O-O bond formation in the final state of the cycle.[15][6]
[NiFe]- and [FeFe]-hydrogenase
Extensive work was performed on the
[NiFe]-Hydrogenase where the magnetic tensors were measured and related to quantum chemical calculations.[11][4] Through his work, the structures of all intermediates in the activation path and catalytic cycle of [NiFe]-hydrogenases were obtained. In the course of this work a 0.89
Ångström resolution
X-ray crystallography diffraction model of [NiFe]-hydrogenase was achieved.[19]
Similar work has been accomplished for the [FeFe]-hydrogenases.[4] A key contribution of his research was the EPR spectroscopic evidence of an azapropane-dithiolate-ligand (ADT-ligand) in the dithiol bridge of the [FeFe]-hydrogenase active site [20] and the determination of the magnitude and orientation of the g-tensor using single crystal EPR.[21] The ADT-ligand was later confirmed by artificial maturation of [FeFe]-hydrogenases.[22] Using artificial maturation, the protein could be generated without the co-factor (
apoprotein) using E. coli
mutagenesis and a synthetically created active site could be inserted,[22][23][24] which has opened new vistas in hydrogenase research.[25]
Awards and recognition
Otto-Klung-Preis für Chemie, FU Berlin (1978)
Max-Kade-Fellowship, New York (1983)
International Zavoisky Award, Russian and Tatarstan Academy of Sciences, Kazan, Russia (2002)
Bruker Prize, Royal Society of Chemistry, ESR group, U.K. (2003)
Fellow of the Royal Society of Chemistry. U.K. (2004)
Gold Medal of the International EPR Society (2005)
Honorary doctorate Dr. h. c., Uppsala University, Sweden (2008)
Fellow of ISMAR (International Society of Magnetic Resonance) (2010)
Foreign Member of the Academy of Sciences of the Republic of Tatarstan (2012)
Honorary doctorate, Dr. h.c., Université d'Aix-Marseille, France (2014)
Robert Bunsen Vorlesung, Deutsche Bunsen-Gesellschaft für Physikalische Chemie e.V. (2017)
Fellow of the International EPR Society (2017)
References
^
abcdLubitz, Wolfgang; Lendzian, Friedhelm; Bittl, Robert (2002). "Radicals, Radical Pairs and Triplet States in Photosynthesis". Accounts of Chemical Research. 35 (5): 313–320.
doi:
10.1021/ar000084g.
ISSN0001-4842.
PMID12020169.
^
abLendzian, F.; Huber, M.; Isaacson, R. A.; Endeward, B.; Plato, M.; Bönigk, B.; Möbius, K.; Lubitz, W.; Feher, G. (1993). "The electronic structure of the primary donor cation radical in Rhodobacter sphaeroides R-26: ENDOR and TRIPLE resonance studies in single crystals of reaction centers". Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1183 (1): 139–160.
doi:
10.1016/0005-2728(93)90013-6.
ISSN0005-2728.
^
abLubitz, W.; Feher, G. (1999). "The primary and secondary acceptors in bacterial photosynthesis III. Characterization of the quinone radicals QA− ⋅ and QB− ⋅ by EPR and ENDOR". Applied Magnetic Resonance. 17 (1): 1–48.
doi:
10.1007/BF03162067.
ISSN0937-9347.
S2CID95064414.
^
abcLubitz, Wolfgang; Reijerse, Eduard; van Gastel, Maurice (2007). "[NiFe] and [FeFe] Hydrogenases Studied by Advanced Magnetic Resonance Techniques". Chemical Reviews. 107 (10): 4331–4365.
doi:
10.1021/cr050186q.
ISSN0009-2665.
PMID17845059.
^Nalepa, A.; Möbius, K.; Lubitz, W.; Savitsky, A. (2014). "High-field ELDOR-detected NMR study of a nitroxide radical in disordered solids: Towards characterization of heterogeneity of microenvironments in spin-labeled systems". Journal of Magnetic Resonance. 242: 203–213.
Bibcode:
2014JMagR.242..203N.
doi:
10.1016/j.jmr.2014.02.026.
ISSN1090-7807.
PMID24685717.
^Cox, N.; Nalepa, A.; Pandelia, M.-E.; Lubitz, W.; Savitsky, A. (2015). "Pulse Double-Resonance EPR Techniques for the Study of Metallobiomolecules". Electron Paramagnetic Resonance Investigations of Biological Systems by Using Spin Labels, Spin Probes, and Intrinsic Metal Ions, Part A. Methods in Enzymology. Vol. 563. pp. 211–249.
doi:
10.1016/bs.mie.2015.08.016.
ISBN9780128028346.
ISSN0076-6879.
PMID26478487.
^Krewald, V.; Retegan, M.; Neese, F.; Lubitz, W.; Pantazis, D. A.; Cox, N. (2016). "Spin State as a Marker for the Structural Evolution of Nature's Water-Splitting Catalyst". Inorganic Chemistry. 55 (2): 488–501.
doi:
10.1021/acs.inorgchem.5b02578.
hdl:1885/230998.
ISSN0020-1669.
PMID26700960.
^Silakov, A.; Wenk, B.; Reijerse, E.J.; Lubitz, W. (2009). "14N HYSCORE investigation of the H-cluster of [FeFe] hydrogenase: evidence for a nitrogen in the dithiol bridge". Physical Chemistry Chemical Physics. 11 (31): 6592–9.
Bibcode:
2009PCCP...11.6592S.
doi:
10.1039/b905841a.
ISSN1463-9076.
PMID19639134.