2005 - Fellow of the Royal Society, United Kingdom
1996 - Royal Netherlands Academy of Arts and Sciences
1996 - Member of the National Academy of Sciences
1994 - Member of Academia Europaea
1988 - Nobel Prize for the determination of the three-dimensional structure of a photosynthetic reaction centre
Hartmut Michel focuses on Photosynthetic reaction centre, Stereochemistry, Crystallography, Cytochrome c oxidase and Photochemistry. His studies deal with areas such as Photosynthetic membrane, Membrane protein complex, Rhodopseudomonas, Bacteriochlorophyll and Photosystem II as well as Photosynthetic reaction centre. His Stereochemistry research is multidisciplinary, incorporating elements of Coenzyme Q – cytochrome c reductase, Protein subunit, Cytochrome, Enzyme and Protein structure.
His Crystallography research integrates issues from Crystallization and Molecule. His research in Cytochrome c oxidase intersects with topics in Proton pump, Paracoccus denitrificans, Cytochrome c and Oxidase test. His Photochemistry research is multidisciplinary, relying on both Electron transport chain, Redox, Cofactor and Active site.
His scientific interests lie mostly in Biochemistry, Stereochemistry, Photosynthetic reaction centre, Crystallography and Cytochrome c oxidase. His work in Biochemistry tackles topics such as Molecular biology which are related to areas like Recombinant DNA, Heterologous expression and Peptide sequence. His work investigates the relationship between Stereochemistry and topics such as Protein subunit that intersect with problems in Amino acid.
His study focuses on the intersection of Photosynthetic reaction centre and fields such as Bacteriochlorophyll with connections in the field of Dimer. His work deals with themes such as Crystallization, Molecule, Hydrogen bond and Protonation, which intersect with Crystallography. His Cytochrome c oxidase study also includes fields such as
His primary scientific interests are in Biochemistry, Stereochemistry, Cytochrome, Respiratory chain and Aquifex aeolicus. His Biochemistry study frequently links to related topics such as Pseudomonas stutzeri. The Stereochemistry study combines topics in areas such as Receptor, Bradykinin, Active site, Heme and Peptide.
The various areas that Hartmut Michel examines in his Cytochrome study include Substrate, Redox, Cytochrome c oxidase and Escherichia coli. Hartmut Michel interconnects Photosynthetic reaction centre and Cytoplasm in the investigation of issues within Substrate. As a member of one scientific family, Hartmut Michel mostly works in the field of Cytochrome c oxidase, focusing on Paracoccus denitrificans and, on occasion, Photochemistry, Catalase and Electron transfer.
The scientist’s investigation covers issues in Biochemistry, Transporter, Oxidase test, Biophysics and Cytochrome c oxidase. While the research belongs to areas of Biochemistry, he spends his time largely on the problem of Pseudomonas stutzeri, intersecting his research to questions surrounding Cytochrome c and Protein subunit. Hartmut Michel has included themes like Integral membrane protein, Membrane protein crystallization and Binding site in his Biophysics study.
His Cytochrome c oxidase study combines topics from a wide range of disciplines, such as Paracoccus denitrificans and Catalase. Hartmut Michel combines subjects such as Cofactor and Heme with his study of Cytochrome. As part of his studies on Active site, Hartmut Michel frequently links adjacent subjects like Stereochemistry.
This overview was generated by a machine learning system which analysed the scientist’s body of work. If you have any feedback, you can contact us here.
Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3Å resolution
Johann Deisenhofer;Otto Epp;Kunio Miki;Robert Huber.
Nature (1985)
Structure at 2.8 A resolution of cytochrome c oxidase from Paracoccus denitrificans.
So Iwata;Christian Ostermeier;Bernd Ludwig;Hartmut Michel.
Nature (1995)
X-ray structure analysis of a membrane protein complex. Electron density map at 3 Å resolution and a model of the chromophores of the photosynthetic reaction center from Rhodopseudomonas viridis
Johann Deisenhofer;Otto Epp;Kunio Miki;Robert Huber.
Journal of Molecular Biology (1984)
The crystal structure of the light-harvesting complex II (B800–850) from Rhodospirillum molischianum
Juergen Koepke;Xiche Hu;Cornelia Muenke;Klaus Schulten.
Structure (1996)
Relevance of the photosynthetic reaction center from purple bacteria to the structure of photosystem II
Hartmut Michel;Johann Deisenhofer.
Biochemistry (1988)
Structure of the photosynthetic reaction centre from Rhodobacter sphaeroides at 2.65 A resolution: cofactors and protein-cofactor interactions
Ulrich Ermler;Günter Fritzsch;Susan K Buchanan;Hartmut Michel.
Structure (1994)
Structure at 2.7 Å resolution of the Paracoccus denitrificans two-subunit cytochrome c oxidase complexed with an antibody FV fragment
Christian Ostermeier;Axel Harrenga;Ulrich Ermler;Hartmut Michel.
Proceedings of the National Academy of Sciences of the United States of America (1997)
The Photosynthetic Reaction Center from the Purple Bacterium Rhodopseudomonas viridis.
Johann Deisenhofer;Hartmut Michel.
Science (1989)
Nobel lecture. The photosynthetic reaction centre from the purple bacterium Rhodopseudomonas viridis
Johann Deisenhofer;Hartmut Michel.
The EMBO Journal (1989)
Structure of a Na + /H + antiporter and insights into mechanism of action and regulation by pH
Carola Hunte;Emanuela Screpanti;Miro Venturi;Abraham Rimon.
Nature (2005)
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