Leonid Sazanov | |
---|---|
Born | Leonid A. Sazanov |
Alma mater | Belarusian State University (MSc) Moscow State University (PhD) |
Awards | EMBO Member (2018) |
Scientific career | |
Fields | Structural biology Bioenergetics Membrane proteins X-ray crystallography Electron microscopy [1] |
Institutions | |
Website | ist |
Leonid A. Sazanov FRS is a professor at the Institute of Science and Technology Austria (ISTA). [1] [2] [3] Sazanov research explores the structure and function of large membrane protein complexes from the domain of bioenergetics. [4] These molecular machines interconvert redox energy and proton motive force across biological membranes using a variety of mechanisms. [4]
Sazanov was educated at the Belarusian State University [5] and Moscow State University, where he was awarded a PhD in 1990. [4]
Sazanov is known for the discovery of the first atomic structure of respiratory complex I, using X-ray crystallography and the bacterial enzyme as a model. [4] It is an entry point into the electron transport chain, responsible for most of the energy production in the cell. [4] The complex I structure revealed many unexpected and unique features of this extravagantly elaborate membrane protein assembly. Sazanov then went on to determine the first complete atomic structure of the even larger mammalian mitochondrial complex I, using new cryogenic electron microscopy methods. [4] [6] [7] [8] [9]
Sazanov research investigates the coupling mechanism of complex I using a combination of structural and biophysical techniques. He is also interested in the structure and mechanism of other membrane-embedded molecular machines in mitochondria and bacteria. [4] [10]
Previously Sazanov served as program leader at the MRC Mitochondrial Biology Unit and research associate at the Medical Research Council (MRC) Laboratory of Molecular Biology. [4] He has been a research fellow at Imperial College London and a postdoctoral researcher at the University of Birmingham. [4]
He was elected a Fellow of the Royal Society (FRS) in 2019 [4] and a member of the European Molecular Biology Organization (EMBO) in 2018. [11]
Oxidative phosphorylation or electron transport-linked phosphorylation or terminal oxidation is the metabolic pathway in which cells use enzymes to oxidize nutrients, thereby releasing chemical energy in order to produce adenosine triphosphate (ATP). In eukaryotes, this takes place inside mitochondria. Almost all aerobic organisms carry out oxidative phosphorylation. This pathway is so pervasive because it releases more energy than alternative fermentation processes such as anaerobic glycolysis.
Respiratory complex I, EC 7.1.1.2 is the first large protein complex of the respiratory chains of many organisms from bacteria to humans. It catalyzes the transfer of electrons from NADH to coenzyme Q10 (CoQ10) and translocates protons across the inner mitochondrial membrane in eukaryotes or the plasma membrane of bacteria.
ATP synthase is a protein that catalyzes the formation of the energy storage molecule adenosine triphosphate (ATP) using adenosine diphosphate (ADP) and inorganic phosphate (Pi). ATP synthase is a molecular machine. The overall reaction catalyzed by ATP synthase is:
Sir John Cowdery Kendrew, was an English biochemist, crystallographer, and science administrator. Kendrew shared the 1962 Nobel Prize in Chemistry with Max Perutz, for their work at the Cavendish Laboratory to investigate the structure of haem-containing proteins.
Sir John Ernest Walker is a British chemist who won the Nobel Prize in Chemistry in 1997. As of 2015 Walker is Emeritus Director and Professor at the MRC Mitochondrial Biology Unit in Cambridge, and a Fellow of Sidney Sussex College, Cambridge.
Richard Henderson is a British 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.„Thanks to his work, we can look at individual atoms of living nature, thanks to cryo-electron microscopes we can see details without destroying samples, and for this he won the Nobel Prize in Chemistry."
Peter Nigel Tripp Unwin FRS is a British scientist at the MRC Laboratory of Molecular Biology, where he was Head of the Neurobiology Division from 1992 until 2008. He is currently also Emeritus Professor of Cell Biology at the Scripps Research Institute.
Modern biological research has revealed strong evidence that the enzymes of the mitochondrial respiratory chain assemble into larger, supramolecular structures called supercomplexes, instead of the traditional fluid model of discrete enzymes dispersed in the inner mitochondrial membrane. These supercomplexes are functionally active and necessary for forming stable respiratory complexes.
Christine Anne Orengo is a Professor of Bioinformatics at University College London (UCL) known for her work on protein structure, particularly the CATH database. Orengo serves as president of the International Society for Computational Biology (ISCB), the first woman to do so in the history of the society.
(Edith) Yvonne JonesFLSW is director of the Cancer Research UK Receptor Structure Research Group at the University of Oxford and a Fellow of Jesus College, Oxford. She is widely known for her research on the molecular biology of cell surface receptors and signalling complexes.
Jan Löwe is a German molecular and structural biologist and the Director of the Medical Research Council (MRC) Laboratory of Molecular Biology (LMB) in Cambridge, UK. He became Director of the MRC-LMB in April 2018, succeeding Sir Hugh Pelham. Löwe is known for his contributions to the current understanding of bacterial cytoskeletons.
Judy Hirst is a British scientist specialising in mitochondrial biology. She is Director of the MRC Mitochondrial Biology Unit at the University of Cambridge.
Lori Anne Passmore is a Canadian/British cryo electron microscopist and structural biologist who works at the Medical Research Council (MRC) Laboratory of Molecular Biology (LMB) at the University of Cambridge. She is known for her work on multiprotein complexes involved in gene expression and development of new supports for cryo-EM.
Neil Alexander Steven Brockdorff is a Wellcome Trust Principal Research Fellow and professor in the department of biochemistry at the University of Oxford. Brockdorff's research investigates gene and genome regulation in mammalian development. His interests are in the molecular basis of X-inactivation, the process that evolved in mammals to equalise X chromosome gene expression levels in XX females relative to XY males.
Vassilis Pachnis Greek: Βασίλης Πάχνης is a Senior Group Leader in the Development and Homeostasis of the Nervous System Laboratory at the Francis Crick Institute.
Sjors Hendrik Willem ScheresFRS is a Dutch scientist at the MRC Laboratory of Molecular Biology Cambridge, UK.
Andrew P. Carter is a British structural biologist who works at the Medical Research Council (MRC) Laboratory of Molecular Biology (LMB) in Cambridge, UK. He is known for his work on the microtubule motor dynein.
Kiyoshi Nagai was a Japanese structural biologist at the MRC Laboratory of Molecular Biology Cambridge, UK. He was known for his work on the mechanism of RNA splicing and structures of the spliceosome.
Caetano Maria Pacheco Pais dos Reis e Sousa is a senior group leader at the Francis Crick Institute and a professor of Immunology at Imperial College London.
Susan Mary Lea is a British biologist who serves as chief of the center for structural biology at the National Cancer Institute. Her research investigates host-pathogen interactions and biomolecular pathways. She was elected a Fellow of the Royal Society in 2022.
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