Hartmut Michel

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Hartmut Michel
Michel, Hartmut (1948).jpg
Hartmut Michel in 2013
Born (1948-07-18) 18 July 1948 (age 70)
Nationality German
Alma mater University of Tübingen
Known forCrystallisation of membrane proteins
Spouse(s)Elena Olkhova
Awards
Scientific career
Fields Biochemistry
Institutions Max Planck Institute for Biophysics
Website www.biophys.mpg.de/en/michel.html

Hartmut Michel (born 18 July 1948) is a German biochemist, who received the 1988 Nobel Prize in Chemistry. [2] [3] [4] [5]

Germany Federal parliamentary republic in central-western Europe

Germany, officially the Federal Republic of Germany, is a country in Central and Western Europe, lying between the Baltic and North Seas to the north, and the Alps to the south. It borders Denmark to the north, Poland and the Czech Republic to the east, Austria and Switzerland to the south, France to the southwest, and Luxembourg, Belgium and the Netherlands to the west.

Biochemist Scientist specialized in biochemistry

Biochemists are scientists that are trained in biochemistry.

Nobel Prize in Chemistry One of the five Nobel Prizes established in 1895 by Alfred Nobel

The Nobel Prize in Chemistry is awarded annually by the Royal Swedish Academy of Sciences to scientists in the various fields of chemistry. It is one of the five Nobel Prizes established by the will of Alfred Nobel in 1895, awarded for outstanding contributions in chemistry, physics, literature, peace, and physiology or medicine. This award is administered by the Nobel Foundation, and awarded by Royal Swedish Academy of Sciences on proposal of the Nobel Committee for Chemistry which consists of five members elected by Academy. The award is presented in Stockholm at an annual ceremony on December 10, the anniversary of Nobel's death.

Contents

Education and early life

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.

Ludwigsburg Place in Baden-Württemberg, Germany

Ludwigsburg is a city in Baden-Württemberg, Germany, about 12 kilometres (7.5 mi) north of Stuttgart city centre, near the river Neckar. It is the largest and primary city of the Ludwigsburg district with about 88,000 inhabitants. It is situated within the Stuttgart Region, and the district is part of the administrative region (Regierungsbezirk) of Stuttgart.

University of Tübingen public research university located in the city of Tübingen, Baden-Württemberg, Germany

The University of Tübingen, officially the Eberhard Karls University of Tübingen, is a public research university located in the city of Tübingen, Baden-Württemberg, Germany.

ATPase dephosphorylation enzyme

ATPases (EC 3.6.1.3, adenylpyrophosphatase, ATP monophosphatase, triphosphatase, SV40 T-antigen, adenosine 5'-triphosphatase, ATP hydrolase, complex V (mitochondrial electron transport), (Ca2+ + Mg2+)-ATPase, HCO3-ATPase, adenosine triphosphatase) are a class of enzymes that catalyze the decomposition of ATP into ADP and a free phosphate ion or the inverse reaction. This dephosphorylation reaction releases energy, which the enzyme (in most cases) harnesses to drive other chemical reactions that would not otherwise occur. This process is widely used in all known forms of life.

Career and research

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. [6]

Membrane protein class of proteins

Membrane proteins are proteins that interact with, or are part of, biological membranes. They include integral membrane proteins that are permanently anchored or part of the membrane and peripheral membrane proteins that are only temporarily attached to the lipid bilayer or to other integral proteins. The integral membrane proteins are classified as transmembrane proteins that span across the membrane and integral monotopic proteins that are attached to only one side of the membrane. Membrane proteins are a common type of proteins along with soluble globular proteins, fibrous proteins, and disordered proteins. They are targets of over 50% of all modern medicinal drugs. It is estimated that 20–30% of all genes in most genomes encode membrane proteins.

X-ray crystallography Technique used in studying crystal structure

X-ray crystallography (XRC) is a technique used for determining the atomic and molecular structure of a crystal, in which the crystalline structure causes a beam of incident X-rays to diffract into many specific directions. By measuring the angles and intensities of these diffracted beams, a crystallographer can produce a three-dimensional picture of the density of electrons within the crystal. From this electron density, the mean positions of the atoms in the crystal can be determined, as well as their chemical bonds, their crystallographic disorder, and various other information.

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.

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.

Frankfurt Place in Hesse, Germany

Frankfurt is a metropolis and the largest city of the German federal state of Hesse, and its 746,878 (2017) inhabitants make it the fifth-largest city of Germany after Berlin, Hamburg, Munich, and Cologne. On the River Main, it forms a continuous conurbation with the neighbouring city of Offenbach am Main, and its urban area has a population of 2.3 million. The city is at the centre of the larger Rhine-Main Metropolitan Region, which has a population of 5.5 million and is Germany's second-largest metropolitan region after the Rhine-Ruhr Region. Since the enlargement of the European Union in 2013, the geographic centre of the EU is about 40 km (25 mi) to the east of Frankfurt's central business district. Like France and Franconia, the city is named after the Franks. Frankfurt is the largest city in the Rhine Franconian dialect area.

Goethe University Frankfurt university in Frankfurt, Germany

University of Frankfurt is a university located in Frankfurt, Germany. It was founded in 1914 as a citizens' university, which means it was founded and funded by the wealthy and active liberal citizenry of Frankfurt. The original name was Universität Frankfurt am Main. In 1932, the university's name was extended in honour of one of the most famous native sons of Frankfurt, the poet, philosopher and writer/dramatist Johann Wolfgang von Goethe. The university currently has around 45,000 students, distributed across four major campuses within the city.

Awards and honours

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. [7] He became a foreign member of the Royal Netherlands Academy of Arts and Sciences in 1995. [8] He was elected a Foreign Member of the Royal Society (ForMemRS) in 2005. [1]

The Gottfried Wilhelm Leibniz Prize is a program of the Deutsche Forschungsgemeinschaft which awards prizes “to exceptional scientists and academics for their outstanding achievements in the field of research.” It was established in 1985 and up to ten prizes are awarded annually to individuals or research groups working at a research institution in Germany or at a German research institution abroad.

Deutsche Forschungsgemeinschaft German research foundation

The Deutsche Forschungsgemeinschaft is a German research funding organization.

Bijvoet Center for Biomolecular Research

The Bijvoet Center for Biomolecular Research is a research institute located 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.

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Kurt Wüthrich Swiss chemist

Kurt Wüthrich is a Swiss chemist/biophysicist and Nobel Chemistry laureate, known for developing nuclear magnetic resonance (NMR) methods for studying biological macromolecules.

Robert Huber German Nobel laureate in chemistry

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.

Photosynthetic reaction centre

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 subsequently 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.

Max Planck Institute of Biophysics research institute

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.

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Roger D. Kornberg American chemist

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Matthias Mann German biochemist and physicist

Matthias Mann is a scientist in the area of mass spectrometry and proteomics. Born in Germany he studied mathematics and physics at the University of Göttingen. He received his Ph.D. in 1988 at Yale University where he worked in the group of John Fenn, who was later awarded the Nobel Prize in Chemistry. After a postdoctoral fellowship at the University of Southern Denmark in Odense he became group leader at the European Molecular Biology Laboratory (EMBL) in Heidelberg. Later he went back to Odense as a professor of bioinformatics. Since 2005 he has been a director at the Max Planck Institute of Biochemistry in Munich. In addition, he will also become a principal investigator at the newly founded "Novo Nordisk Foundation Center for Protein Research" in Copenhagen.

Johannes Martin Bijvoet Dutch crystallographer

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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 protein family InterPro Family

Photosynthetic reaction centre proteins are main protein components of photosynthetic reaction centres of bacteria and plants.

Bacterial antenna complex

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.

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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.

References

  1. 1 2 "Professor Hartmut Michel ForMemRS". London: Royal Society. Archived from the original on 2015-10-26.
  2. Autobiographical information on Hartmut at www.nobel.org
  3. Structural genomics on selected families of secondary active transporters, project page at the Frankfurt University
  4. Iwata, S.; Ostermeier, C.; Ludwig, B.; Michel, H. (1995). "Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans". Nature. 376 (6542): 660. doi:10.1038/376660a0.
  5. Deisenhofer, J.; Epp, O.; Miki, K.; Huber, R.; Michel, H. (1984). "X-ray structure analysis of a membrane protein complex". Journal of Molecular Biology. 180 (2): 385. doi:10.1016/S0022-2836(84)80011-X.
  6. 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 (6047): 618. doi:10.1038/318618a0.
  7. "Bijvoet Medal". Bijvoet Center for Biomolecular Research. Retrieved 2017-09-12.
  8. "H. Michel". Royal Netherlands Academy of Arts and Sciences. Archived from the original on 13 February 2016. Retrieved 13 February 2016.