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MRC Mitochondrial Biology Unit


John Walker FRS, FMedSci

Emeritus Director

Nobel Laureate






Mitochondrial ATP synthase: cellular power generator, determinant of mitochondrial cristae formation, a site linked to human diseases

Energy from the sun is entrapped by photosynthesis and stored in high energy compounds that we consume in food. The energy is released by controlled burning in the mitochondria in the cells of our bodies, and stored in the high energy compound adenosine triphosphate, ATP, the fuel of biology. ATP is made in the mitochondria inside our cells. They are “power stations” full of millions of molecular turbines, the ATP synthases that rotate like man-made turbines and churn out ATP in massive quantities.

We understand most of how these molecular turbines work, but not how rotation is generated. This project will provide the missing information. Bacteria have turbines that differ significantly from the human ones, and they are controlled by different mechanisms. We want to understand these differences in structure, function and regulation so as to devise drugs to kill pathogenic bacteria by stopping their turbines without influencing the human ones.


John Walker studied chemistry at the Sir William Dunn School of Pathology, University of Oxford, where he obtained a BA in Chemistry, Sir William Dunn School of Pathology (1965) and a DPhil in Biochemistry, St Catherine's College (1969). Previously, John attended Rastrick Grammar School, Brighouse, West Yorkshire from 1953 until 1960, where he was awarded the A. T. Clay Gold Medal for academic distinction.  A leading figure in the world of biochemistry, John received the 1997 Nobel Prize in Chemistry for his work on ATP synthase, the complex enzyme responsible for the formation of ATP, uncovering its key structural features. He was knighted for his services to science in 1999. Amongst his numerous other accolades, he has received the Biochemical Society’s Keilin Medal, as well as the 2012 Copley Medal of the Royal Society. He is a Founding Fellow of the Academy of Medical Sciences (FMedSci) and, in 2021, the University of Cambridge awarded him the Honorary Degree of Doctor of Science honoris causa. John is a Fellow of Sidney Sussex College.

Further biographical details


Selected Publications

Hirst J, Kunji ERS & Walker JE (2019)
Comment on "Protein assemblies ejected directly from native membranes yield complexes for mass spectrometry".
Science, 366, eaaw9830

Petri J, Nakatani Y, Montgomery MG, Ferguson SA, Aragão D, Leslie AGW, Heikal A, Walker JE & Cook GM (2019)
Structure of F-ATPase from the obligate anaerobe Fusobacterium nucleatum.
Open Biol 9, 190066

Carroll J, He J, Ding S, Fearnley IM & Walker JE (2019)
Persistence of the permeability transition pore in human mitochondria devoid of an assembled ATP synthase.
Proc Natl Acad Sci U S A 116, 12816-12821

Boreikaite V, Wicky BIM, Watt IN, Clarke J & Walker JE (2019)
Extrinsic conditions influence the self-association and structure of IF, the regulatory protein of mitochondrial ATP synthase.
Proc Natl Acad Sci U S A 116, 10354-10359

Gahura O, Šubrtová K, Váchová H, Panicucci B, Fearnley IM, Harbour ME, Walker JE & Zíková A (2018)
The F -ATPase from Trypanosoma brucei is elaborated by three copies of an additional p18-subunit.
FEBS J 285, 614-628

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PubMed (last 10 years)