Sir John Walker | |
---|---|
Born | John Ernest Walker 7 January 1941 [1] Halifax, West Riding of Yorkshire, England |
Education | Rastrick Grammar School |
Alma mater | University of Oxford |
Spouse | Christina Westcott (m. 1963) |
Children | Two |
Awards |
|
Scientific career | |
Institutions | University of Oxford Laboratory of Molecular Biology University of Cambridge |
Thesis | Studies on naturally occurring peptides (1970) |
Doctoral advisor | Edward Abraham [4] |
Website | www |
Sir John Ernest Walker (born 7 January 1941) is a British chemist who won the Nobel Prize in Chemistry in 1997. [5] As of 2015 [update] Walker is Emeritus Director and Professor at the MRC Mitochondrial Biology Unit in Cambridge, and a Fellow of Sidney Sussex College, Cambridge. [6] [7] [8] [9] [10]
Walker was born in Halifax, Yorkshire, the son of Thomas Ernest Walker, a stonemason, and Elsie Lawton, an amateur musician. He was brought up with his two younger sisters (Judith and Jen) in a rural environment and went to Rastrick Grammar School. At school, he was a keen sportsman and specialized in physical sciences and mathematics during his final three years there. He received a 3rd class Bachelor of Arts degree in chemistry from St Catherine's College, Oxford. [11] [12] Walker began his study of peptide antibiotics with Edward Abraham at Oxford in 1965 and received his Doctor of Philosophy degree in 1969. [4] [11] During this period, he became interested in developments in molecular biology.
From 1969 to 1971, Walker worked at the University of Wisconsin–Madison, and from 1971 to 1974 in France. He met Fred Sanger [13] in 1974 at a workshop at the University of Cambridge. This resulted in an invitation to work at the Laboratory of Molecular Biology of the Medical Research Council, which became a long-term appointment. Among the other staff was Francis Crick, who was well known for his discovery of the molecular structure of DNA. At first, he analyzed the sequences of proteins and then uncovered details of the modified genetic code in mitochondria. In 1978, he decided to apply protein chemical methods to membrane proteins. In this way, Walker characterized the subunit composition of proteins in the mitochondrial membrane and the DNA sequence of the mitochondrial genome.
His landmark crystallographic studies of the F1-ATPase, the catalytic region of the ATP synthase (done in collaboration with crystallographer Andrew Leslie), from bovine heart mitochondria revealed the three catalytic sites in three different conformations imposed by the position of the asymmetric central stalk. This structure supported the binding change mechanism and rotary catalysis for the ATP synthase (and related enzymes), one of the catalytic mechanisms proposed by Paul Boyer. This work, published in 1994, led to Walker's share of the 1997 Nobel prize for chemistry. Since this structure, Walker and his colleagues have produced most of the crystal structures in the PDB of mitochondrial ATP synthase, including transition state structures and protein with bound inhibitors and antibiotics. Scientists trained in Walker's group at the MRC Laboratory of Molecular Biology in Cambridge or MRC Mitochondrial Biology Unit have gone on to determine crystal bacterial complex I and cryo-EM maps of mitochondrial complex I and vacuolar type ATPases.
Many students and postdoctoral research fellows who studied with John Walker have gone on to independent research careers, including Leonid Sazanov, Postdoctoral Fellow (ISTA) and Daniela Stock, Postdoctoral Fellow (Sydney).
Walker was elected an EMBO Member in 1984. [14] He shared his Nobel Prize with the American chemist Paul D. Boyer for their elucidation of the enzymatic mechanism underlying the synthesis of adenosine triphosphate. They also shared the prize with Danish chemist Jens C. Skou for research unrelated to theirs (Discovery of the Na+/K+-ATPase). Sir John was knighted in 1999 for services to molecular biology. He is a member of the Advisory Council for the Campaign for Science and Engineering. [15] He was elected a Fellow of the Royal Society (FRS) in 1995. [3] Walker is also a Foreign Associate of the National Academy of Sciences and an Honorary Fellow of St Catherine's College, Oxford. [16] He became a foreign member of the Royal Netherlands Academy of Arts and Sciences in 1999. [17] In 2012 he was awarded the Copley Medal. [3]
Walker married Christina Westcott in 1963, and has two daughters. [2]
ATPases (EC 3.6.1.3, Adenosine 5'-TriPhosphatase, adenylpyrophosphatase, ATP monophosphatase, triphosphatase, SV40 T-antigen, 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.
ATP synthase is an enzyme 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:
Paul Delos Boyer was an American biochemist, analytical chemist, and a professor of chemistry at University of California, Los Angeles (UCLA). He shared the 1997 Nobel Prize in Chemistry for research on the "enzymatic mechanism underlying the biosynthesis of adenosine triphosphate (ATP)" with John E. Walker, making Boyer the first Utah-born Nobel laureate; the remainder of the Prize in that year was awarded to Danish chemist Jens Christian Skou for his discovery of the Na+/K+-ATPase.
Sir Richard John Roberts is a British biochemist and molecular biologist. He was awarded the 1993 Nobel Prize in Physiology or Medicine with Phillip Allen Sharp for the discovery of introns in eukaryotic DNA and the mechanism of gene-splicing. He currently works at New England Biolabs.
Sir Gregory Paul Winter is a Nobel Prize-winning English molecular biologist best known for his work on the therapeutic use of monoclonal antibodies. His research career has been based almost entirely at the MRC Laboratory of Molecular Biology and the MRC Centre for Protein Engineering, in Cambridge, England.
Michael Levitt, is a South African-born biophysicist and a professor of structural biology at Stanford University, a position he has held since 1987. Levitt received the 2013 Nobel Prize in Chemistry, together with Martin Karplus and Arieh Warshel, for "the development of multiscale models for complex chemical systems". In 2018, Levitt was a founding co-editor of the Annual Review of Biomedical Data Science.
Martin Karplus is an Austrian and American theoretical chemist. He is the Director of the Biophysical Chemistry Laboratory, a joint laboratory between the French National Center for Scientific Research and the University of Strasbourg, France. He is also the Theodore William Richards Professor of Chemistry, emeritus at Harvard University. Karplus received the 2013 Nobel Prize in Chemistry, together with Michael Levitt and Arieh Warshel, for "the development of multiscale models for complex chemical systems".
The Medical Research Council (MRC) Laboratory of Molecular Biology (LMB) is a research institute in Cambridge, England, involved in the revolution in molecular biology which occurred in the 1950–60s. Since then it has remained a major medical research laboratory at the forefront of scientific discovery, dedicated to improving the understanding of key biological processes at atomic, molecular and cellular levels using multidisciplinary methods, with a focus on using this knowledge to address key issues in human health.
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."
ATP synthase F1 subunit alpha, mitochondrial is an enzyme that in humans is encoded by the ATP5F1A gene.
ATP synthase subunit delta, mitochondrial, also known as ATP synthase F1 subunit delta or F-ATPase delta subunit is an enzyme that in humans is encoded by the ATP5F1D gene. This gene encodes a subunit of mitochondrial ATP synthase. Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation.
Laurence Harris Pearl FRS FMedSci is a British biochemist and structural biologist who is currently Professor of Structural Biology in the Genome Damage and Stability Centre and was Head of the School of Life Sciences at the University of Sussex.
Dario Renato Alessi is a French-born British biochemist, Director of the Medical Research Council Protein Phosphorylation and Ubiquitylation Unit and Professor of Signal Transduction, at the School of Life Sciences, University of Dundee.
James Henderson Naismith is a Scot, Professor of Structural Biology and since autumn of 2023 the Head of the Mathematical, Physical, and Life Science Division (MPLS) Division at the University of Oxford. He was the inaugural Director of the Rosalind Franklin Institute and Director of the Research Complex at Harwell. He previously served as Bishop Wardlaw Professor of Chemical Biology at the University of St Andrews. He was a member of Council of the Royal Society (2021-2022). He is also currently the Vice-Chair of Council of the European X-ray Free Electron Laser and Vice-President (non-clinical) of The Academy of Medical Sciences.
Edith Yvonne Jones is a British molecular biologist who 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.
Sir Richard Henry Treisman is a British scientist specialising in the molecular biology of cancer. Treisman is a director of research at the Francis Crick Institute in London.
Leonid A. Sazanov is a professor at the Institute of Science and Technology Austria (ISTA). Sazanov research explores the structure and function of large membrane protein complexes from the domain of bioenergetics. These molecular machines interconvert redox energy and proton motive force across biological membranes using a variety of mechanisms.
M. Madan Babu is an Indian-American computational biologist and bioinformatician. He is the endowed chair in biological data science and director of the center of excellence for data-driven discovery at St. Jude Children's Research Hospital. Previously, he served as a programme leader at the MRC Laboratory of Molecular Biology (LMB).
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