Hartmut Michel in 2013
|Alma mater||University of Tübingen|
|Known for||Crystallisation of membrane proteins|
|Institutions||Max Planck Institute for Biophysics|
Hartmut Michel (born 18 July 1948) is a German biochemist, who received the 1988 Nobel Prize in Chemistry for determination of the first crystal structure of an integral membrane protein, a membrane-bound complex of proteins and co-factors that is essential to photosynthesis.
He was born on 18 July 1948 in Ludwigsburg. After compulsory military service, he studied biochemistry at the University of Tübingen, working for his final year at Dieter Oesterhelt's laboratory on ATPase activity of halobacteria.
Hartmut later[ when? ] worked on the crystallisation of membrane proteins - essential for their structure elucidation by X-ray crystallography. He received the Nobel Prize jointly with Johann Deisenhofer and Robert Huber in 1988. Together with Michel and Huber, Deisenhofer determined the three-dimensional structure of a protein complex found in certain photosynthetic bacteria. This membrane protein complex, called a photosynthetic reaction center, was known to play a crucial role in initiating a simple type of photosynthesis. Between 1982 and 1985, the three scientists used X-ray crystallography to determine the exact arrangement of the more than 10,000 atoms that make up the protein complex. Their research increased the general understanding of the mechanisms of photosynthesis, revealed similarities between the photosynthetic processes of plants and bacteria and established a methodology for crystallising membrane proteins.
Since 1987 he has been director of the Molecular Membrane Biology department at the Max Planck Institute for Biophysics in Frankfurt am Main, Germany, and professor of biochemistry at the Goethe University Frankfurt.
In 1986, he received the Gottfried Wilhelm Leibniz Prize of the Deutsche Forschungsgemeinschaft, which is the highest honour awarded in German research. In 1988, he received the Nobel Prize in Chemistry. He received the Bijvoet Medal at the Bijvoet Center for Biomolecular Research of Utrecht University in 1989.He became a foreign member of the Royal Netherlands Academy of Arts and Sciences in 1995. He was elected a Foreign Member of the Royal Society (ForMemRS) in 2005.
Kurt Wüthrich is a Swiss chemist/biophysicist and Nobel Chemistry laureate, known for developing nuclear magnetic resonance (NMR) methods for studying biological macromolecules.
Johann Deisenhofer is a German biochemist who, along with Hartmut Michel and Robert Huber, received the Nobel Prize for Chemistry in 1988 for their determination of the first crystal structure of an integral membrane protein, a membrane-bound complex of proteins and co-factors that is essential to photosynthesis.
Robert Huber is a German biochemist and Nobel laureate. known for his work crystallizing an intramembrane protein important in photosynthesis and subsequently applying X-ray crystallography to elucidate the protein's structure.
A photosynthetic reaction center is a complex of several proteins, pigments and other co-factors that together execute the primary energy conversion reactions of photosynthesis. Molecular excitations, either originating directly from sunlight or transferred as excitation energy via light-harvesting antenna systems, give rise to electron transfer reactions along the path of a series of protein-bound co-factors. These co-factors are light-absorbing molecules such as chlorophyll and phaeophytin, as well as quinones. The energy of the photon is used to excite an electron of a pigment. The free energy created is then used to reduce a chain of nearby electron acceptors, which have progressively higher redox-potentials. These electron transfer steps are the initial phase of a series of energy conversion reactions, ultimately resulting in the conversion of the energy of photons to the storage of that energy by the production of chemical bonds.
A chlorosome is a photosynthetic antenna complex found in green sulfur bacteria (GSB) and some green filamentous anoxygenic phototrophs (FAP). They differ from other antenna complexes by their large size and lack of protein matrix supporting the photosynthetic pigments. Green sulfur bacteria are a group of organisms that generally live in extremely low-light environments, such as at depths of 100 metres in the Black Sea. The ability to capture light energy and rapidly deliver it to where it needs to go is essential to these bacteria, some of which see only a few photons of light per chlorophyll per day. To achieve this, the bacteria contain chlorosome structures, which contain up to 250,000 chlorophyll molecules. Chlorosomes are ellipsoidal bodies, in GSB their length varies from 100 to 200 nm, width of 50-100 nm and height of 15 - 30 nm, in FAP the chlorosomes are somewhat smaller.
The Max Planck Institute of Biophysics is located in Frankfurt am Main, Germany. It was founded as Kaiser Wilhelm Institute for Biophysics in 1937, and moved into a new building in 2003. It is one of 80 institutes in the Max Planck Society. Since April 2003, the institute's four departments are housed in the same building, resulting in improved scientific interaction between the research groups. Scientific links to fellow researchers at Frankfurt University have been strengthened further as the institute is now situated next to the University's biology, chemistry and physics laboratories. Together with the Max Planck Institute for Brain Research and the Goethe University of Frankfurt am Main the institute runs the International Max Planck Research School (IMPReS) on the Structure and Function of Biological Membranes, a graduate program offering a Ph.D.
Richard Henderson is a Scottish molecular biologist and biophysicist and pioneer in the field of electron microscopy of biological molecules. Henderson shared the Nobel Prize in Chemistry in 2017 with Jacques Dubochet and Joachim Frank.
Roger David Kornberg is an American biochemist and professor of structural biology at Stanford University School of Medicine. Kornberg was awarded the Nobel Prize in Chemistry in 2006 for his studies of the process by which genetic information from DNA is copied to RNA, "the molecular basis of eukaryotic transcription."
Johannes Martin Bijvoet was a Dutch chemist and crystallographer at the van 't Hoff Laboratory at Utrecht University. He is famous for devising a method of establishing the absolute configuration of molecules. In 1946 he became member of the Royal Netherlands Academy of Arts and Sciences.
Wolfram Saenger is a German biochemist and protein crystallographer. In his research career spanning over 30 years he has worked at the Max Planck Institute for Experimental Medicine, Harvard University and the Free University of Berlin, where he led the Institute for Crystallography research until his retirement in 2011. A recipient of the Gottfried Wilhelm Leibniz Prize (1987) of the Deutsche Forschungsgemeinschaft, which is the highest honor awarded for achievements in research in Germany, and the Humboldt Prize (1988), he is best known for his research on X-ray crystallography of membrane proteins and protein-nucleic acid complexes. He has authored 10 books, including the venerated book 'Principles of Nucleic Acid Structure' published by Springer, and over 500 scientific articles.
Photosynthetic reaction centre proteins are main protein components of photosynthetic reaction centres (RCs) of bacteria and plants. They are transmembrane proteins embedded in the chloroplast thylakoid or bacterial cell membrane.
Bacterial antenna complex proteins are the main light-absorbing components in photosynthetic bacteria. Also known as a light-harvesting complex/system, the bacterial antenna complex is responsible for the transfer of solar energy to the photosynthetic reaction centre.
Isabella Karle was an American chemist who was instrumental in developing techniques to extract plutonium chloride from a mixture containing plutonium oxide. For her scientific work, Karle received the Garvan–Olin Medal, Gregori Aminoff Prize, Bower Award, National Medal of Science, and the Navy Distinguished Civilian Service Award.
Piet Gros is a Dutch chemist and professor biomacromolecular crystallography at Utrecht University. In 2010 he received the NWO Spinoza Prize for the elucidation of the three-dimensional structure of the C3 protein, which plays a central role in the complement system and contributes to innate immunity.
The Bijvoet Center for Biomolecular Research is a research institute at Utrecht University. The Bijvoet Center performs research on the relation between the structure and function of biomolecules, including proteins and lipids, which play a role in biological processes such as regulation, interaction and recognition. The Bijvoet Center houses advanced infrastructures for the analysis of proteins and other biomolecules using NMR, X-ray crystallography, electron microscopy and mass spectrometry. The institute is named after famous Dutch chemist Johannes Martin Bijvoet, who worked at Utrecht University.
Biomolecular complex, also called macromolecular complex or biomacromolecular complex, is any biological complex made of more than one molecule of protein, RNA, DNA, lipids, or carbohydrates. The interactions between these biomolecules are non-covalent. Examples:
Klaus Schulten was a German-American computational biophysicist and the Swanlund Professor of Physics at the University of Illinois at Urbana-Champaign. Schulten used supercomputing techniques to apply theoretical physics to the fields of biomedicine and bioengineering and dynamically model living systems. His mathematical, theoretical, and technological innovations led to key discoveries about the motion of biological cells, sensory processes in vision, animal navigation, light energy harvesting in photosynthesis, and learning in neural networks.
Maria-Elisabeth Michel-Beyerle is a German chemist. From 1974-2000 she was a professor of Physical Chemistry at the Technical University of Munich. Among other awards, she has received the 2000 Bavarian Order of Merit, the highest service order bestowed by the Free State of Bavaria, for her work on photosynthesis.
Marc Baldus is a physicist and professor of NMR spectroscopy at Utrecht University. He is especially known for his work in the field of structural biology using solid-state nuclear magnetic resonance (ssNMR) spectroscopy. He applies ssNMR methods to establish structure-function relationships in complex biomolecular systems including membrane and Amyloid proteins. In addition, he develops cellular NMR methods to study large molecular transport and insertion systems in bacteria as well as signal transduction mechanisms in eukaryotic cells.