Judy Hirst

Last updated

Judy Hirst
FRS FMedSci
Education
Alma mater University of Oxford
AwardsFellow of the Academy of Medical Sciences (2019)
Scientific career
Institutions University of Cambridge
Scripps Research Institute
Thesis Electron transport in redox enzymes  (1997)
Doctoral advisor Fraser Armstrong [1]
Website www.mrc-mbu.cam.ac.uk/research-groups/hirst-group

Judy Hirst is a British scientist specialising in mitochondrial biology. She is Director [2] of the MRC Mitochondrial Biology Unit at the University of Cambridge.

Contents

Early life and education

Hirst grew up in Lepton, a village near Huddersfield, West Yorkshire, and attended King James's School and Greenhead College, Huddersfield. [3] She studied for an M.A. in chemistry at St John's College, Oxford, [2] and then was awarded a Doctor of Philosophy degree at Lincoln College, Oxford, in 1997, for research supervised by Fraser Armstrong on electron transport in redox enzymes. [1]

Career and research

Following her D.Phil., Hirst held a fellowship at the Scripps Research Institute in California, before moving to Cambridge. [4]

As of 2023 Hirst is a professorial fellow and Director of Studies in Natural Sciences Chemistry at Corpus Christi College, Cambridge, [4] and since 2020 has been director of the MRC Mitochondrial Biology Unit having previously been its assistant director (2011-2014) and deputy director (2014-2020). Her main research interest is mitochondrial complex I. [2]

Hirst has been published in 2018 on Open questions: respiratory chain supercomplexes – why are they there and what do they do? [5] and working with Justin Fedor, published research on mitochondrial supercomplexes in Cell Metabolism . [6] Recent research in her team includes a study, published in May 2020 by the American Chemical Society Synthetic Biology on 'Adenosine triphosphate (ATP), the cellular energy currency, is essential for life. The ability to provide a constant supply of ATP is therefore crucial for the construction of artificial cells in synthetic biology' which has developed a 'minimal system for cellular respiration and energy regeneration'. [7]

Awards and honours

Early in her career, Hirst was awarded EMBO Young Investigator Award (2001) and Young Investigator Award from the Royal Society of Chemistry Inorganic Biochemistry Discussion Group (2006). [8]

Hirst was elected a Fellow of the Royal Society (FRS) in 2018. [9] She was awarded an Interdisciplinary Prize of the Royal Society of Chemistry in the same year. [10] In 2019, Hirst was elected Fellow of the Academy of Medical Sciences [11] with the citation:

Judy Hirst, Professor of Biological Chemistry at the MRC Mitochondrial Biology Unit, Cambridge, has had a definitive hand in every advance towards defining the highly complex mechanism of complex I catalysis, and has developed new physical and biochemical methods to address the elusive coupling mechanism between the redox reaction and proton translocation. She established the mechanism of complex I inhibition by the anti-diabetic drug metformin, and has used kinetic and thermodynamic strategies to define how superoxide production by complex I, responds to the intramitochondrial NADH/NAD+ ratio to directly link two pathological effects of complex I dysfunction. This seminal work has brought understanding that is fundamental to critical issues of health and disease on a global stage. [12]

Hirst was awarded Keilin Memorial Lecture and Medal in 2020 for research which:

has made pivotal contributions to understanding energy conversion in complex redox enzymes: how they capture the energy released by a redox reaction to power proton translocation across a membrane, or catalyse the interconversion of chemical bond energy and electrical potential. She is known particularly for her work on mammalian respiratory complex I (NADH: ubiquinone oxidoreductase), an energy-transducing, mitochondrial redox enzyme of fundamental and medical importance, and for solving its structure by electron cryomicroscopy. [13] [14]

Related Research Articles

<span class="mw-page-title-main">Cytochrome</span> Redox-active proteins containing a heme with a Fe atom as a cofactor

Cytochromes are redox-active proteins containing a heme, with a central iron (Fe) atom at its core, as a cofactor. They are involved in the electron transport chain and redox catalysis. They are classified according to the type of heme and its mode of binding. Four varieties are recognized by the International Union of Biochemistry and Molecular Biology (IUBMB), cytochromes a, cytochromes b, cytochromes c and cytochrome d.

<span class="mw-page-title-main">Oxidative phosphorylation</span> Metabolic pathway

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.

An electron transport chain (ETC) is a series of protein complexes and other molecules which transfer electrons from electron donors to electron acceptors via redox reactions (both reduction and oxidation occurring simultaneously) and couples this electron transfer with the transfer of protons (H+ ions) across a membrane. Many of the enzymes in the electron transport chain are embedded within the membrane.

<span class="mw-page-title-main">Respiratory complex I</span> Protein complex involved in cellular respiration

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.

Greenhead College is a sixth form college, and former grammar school, located in Huddersfield, in the county of West Yorkshire, England. The current principal is Mo Bunter. With over 2,700 students, it is a large sixth form college, attracting students from as far afield as Wakefield, Manchester, Barnsley, Bradford, Leeds, Halifax, Wetherby and even Wales. It is located next to Greenhead Park which is one of the largest parks in Huddersfield.

<span class="mw-page-title-main">Alan Fersht</span> British chemist (born 1943)

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<span class="mw-page-title-main">Peter D. Mitchell</span> British biochemist

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<span class="mw-page-title-main">John E. Walker</span> British chemist (born 1941)

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.

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<span class="mw-page-title-main">Richard Henderson (biologist)</span> British biologist (born 1945)

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<span class="mw-page-title-main">MRC Mitochondrial Biology Unit</span> Cambridge University medical school department

The MRC Mitochondrial Biology Unit is a department of the School of Clinical Medicine at the University of Cambridge, funded through a strategic partnership between the Medical Research Council and the University. It is located at the Addenbrooke’s Hospital / Cambridge Biomedical Campus site in Cambridge, England. The unit is concerned with the study of the mitochondrion, as this organelle has a varied and critical role in many aspects of eukaryotic metabolism and is implicated in many metabolic, degenerative, and age-related human diseases.

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<span class="mw-page-title-main">NDUFB11</span> Protein-coding gene in the species Homo sapiens

NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mitochondrial is an enzyme that in humans is encoded by the NDUFB11 gene. NADH dehydrogenase (ubiquinone) 1 beta subcomplex subunit 11 is an accessory subunit of the NADH dehydrogenase (ubiquinone) complex, located in the mitochondrial inner membrane. It is also known as Complex I and is the largest of the five complexes of the electron transport chain. NDUFB11 mutations have been associated with linear skin defects with multiple congenital anomalies 3 and mitochondrial complex I deficiency.

Fraser Andrew Armstrong is a professor of chemistry at the University of Oxford and a Fellow of St John's College, Oxford.

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<span class="mw-page-title-main">Supercomplex</span>

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<span class="mw-page-title-main">James Naismith (chemist)</span> British structural biologist

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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.

References

  1. 1 2 Hirst, Judy (1997). Electron transport in redox enzymes. bodleian.ox.ac.uk (DPhil thesis). University of Oxford. OCLC   557413704. EThOS   uk.bl.ethos.364043.
  2. 1 2 3 "Judy Hirst FRS | MRC Mitochondrial Biology Unit". www.mrc-mbu.cam.ac.uk. Archived from the original on 8 May 2019. Retrieved 16 August 2020.
  3. ↑ "Dr Judy Hirst MA, DPhil, FRS". www.greenhead.ac.uk. Retrieved 16 August 2020.
  4. 1 2 "Dr Judy Hirst MA DPhil (Oxford) FRS FMedSci". Corpus Christi College. Retrieved 3 July 2023.
  5. ↑ Hirst, Judy (2018). "Open questions: respiratory chain supercomplexes-why are they there and what do they do?". BMC Biol. 16 (1): 111. doi: 10.1186/s12915-018-0577-5 . ISSN   1741-7007. PMC   6211484 . PMID   30382836.
  6. ↑ Fedor, Justin; Hirst, Judy (2018). "Mitochondrial Supercomplexes Do Not Enhance Catalysis by Quinone Channeling". Cell Metab. 28 (3): 525–531.e4. doi: 10.1016/j.cmet.2018.05.024 . ISSN   1932-7420. PMC   6125145 . PMID   29937372.
  7. ↑ Biner, Olivier; Fedor, Justin G.; Yin, Zhan; Hirst, Judy (19 June 2020). "Bottom-Up Construction of a Minimal System for Cellular Respiration and Energy Regeneration". ACS Synthetic Biology. 9 (6): 1450–1459. doi: 10.1021/acssynbio.0c00110 . PMC   7611821 . PMID   32383867.
  8. ↑ "RSC Interdisciplinary Prize 2018 Winner". www.rsc.org. Retrieved 16 August 2020.
  9. ↑ "Judy Hirst". royalsociety.org. Retrieved 10 May 2018.
  10. ↑ "2018 Interdisciplinary Prize Winner: Dr Judy Hirst". Royal Society of Chemistry. Retrieved 10 May 2018.
  11. ↑ "New Fellows: 50 top biomedical and health scientists join the Academy | The Academy of Medical Sciences". acmedsci.ac.uk. Retrieved 16 August 2020.
  12. ↑ "Professor Judy Hirst | The Academy of Medical Sciences". acmedsci.ac.uk. Retrieved 16 August 2020.
  13. ↑ "The Keilin Memorial Lecture". www.biochemistry.org. Retrieved 3 July 2023.
  14. ↑ "Professor Judy Hirst FRS receives Keilin Memorial Lecture Award". Corpus Christi College University of Cambridge. 1 April 2019. Retrieved 16 August 2020.
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