S. Samar Hasnain Explained

S. Samar Hasnain FInstP, FRSC, is the inaugural Max Perutz professor of Molecular Biophysics at the University of Liverpool. In 1991 he became a Fellow of the Institute of Physics and in 2002 he became a Fellow of the Royal Society of Chemistry. In 1997 he became a Fellow of the Third World Academy of Sciences. He became Foreign Fellows of Pakistan Academy of Sciences in 2017.[1]

Education

In 1970 Hasnain earned a Bachelor of Science (Honours) an M.Sc. in 1972 from the University of Karachi and a Ph.D. in 1976 from the University of Manchester on Molecular Crystals, using synchrotron radiation from the NINA facility.

Career and Research

After spending a year as Post-Doctoral Research Associate at Manchester he joined DESY in Hamburg as a DESY Fellow working on the Storage ring Synchrotron Radiation Facility, where the synchrotron team created HASYLAB in 1978.

In 1979, Professor Hasnain joined the Daresbury Laboratory as a member of the team establishing the world’s first dedicated X-Ray synchrotron radiation source (the SRS). In 1989, he established the Molecular Biophysics group at Daresbury, where he remained as head of the group until March 2008 when he moved to the University of Liverpool. During 2011-2105 he was the International Lead for the Faculty of Health and Life Sciences of the university.

In 1982, Hasnain helped Perutz to resolve a controversy in the mechanism of oxygen uptake by haemoglobin.[2] [3] [4]

He is the founding Editor of the International Union of Crystallography’s (IUCr) Journal of Synchrotron Radiation in 1993 and was Editor in Chief of IUCr Journals from 2012 to 2018. In 2014, he launched the IUCr’s flagship journal IUCrJ. He is a member of the International Advisory Board for IUCrJ. He is also an Editor of the journal Current opinion in Structural Biology.

He has been engaged with the SESAME synchrotron project in Jordan, launched under the umbrella of UNESCO, since its inception in 2004 and has been the UK Government’s representative on its council since its foundation. He has been chair of its Programme Review committee since 2018.[5]

His main research interest is in structure-function studies of proteins and their complexes that are involved in biological electron transfer,[6] nitrogen cycles[7] [8] [9] [10] [11]

Notes and References

  1. Web site: Pakistan Academy of Sciences | Fellow Profile .
  2. Stereochemistry of iron in deoxyhaemoglobin . 10.1038/295535a0 . 1982 . Perutz . M. F. . Hasnain . S. Samar . Duke . P. J. . Sessler . J. L. . Hahn . J. E. . Nature . 295 . 5849 . 535–538 . 7057913 . 1982Natur.295..535P . 4309029 .
  3. Science is Not a Quiet Life, Max Perutz, 1998, (hardcover), (softcover), (ebook)
  4. Architects of Structural Biology: Bragg, Perutz, Kendrew, Hodgkin, John Meurig Thomas, 2020, .
  5. Web site: Samar Hasnain – UNESCO in the UK. 2020-08-04. en-US.
  6. 10.1038/nature11996 . Structures of protein–protein complexes involved in electron transfer . 2013 . Antonyuk . Svetlana V. . Han . Cong . Eady . Robert R. . Hasnain . S. Samar . Nature . 496 . 7443 . 123–126 . 23535590 . 3672994 . 2013Natur.496..123A .
  7. 10.1038/ncomms5395 . Impact of residues remote from the catalytic centre on enzyme catalysis of copper nitrite reductase . 2014 . Leferink . Nicole G. H. . Antonyuk . Svetlana V. . Houwman . Joseline A. . Scrutton . Nigel S. . Eady . Robert R. . Hasnain . S. Samar . Nature Communications . 5 . 4395 . 25022223 . 4104443 . 2014NatCo...5.4395L .
  8. 10.1073/pnas.0504207102 . Atomic resolution structures of resting-state, substrate- and product-complexed Cu-nitrite reductase provide insight into catalytic mechanism . 2005 . Antonyuk . Svetlana V. . Strange . Richard W. . Sawers . Gary . Eady . Robert R. . Hasnain . S. Samar . Proceedings of the National Academy of Sciences . 102 . 34 . 12041–12046 . 16093314 . 1189323 . 2005PNAS..10212041A . free .
  9. X-ray structure of a blue-copper nitrite reductase in two crystal forms. The nature of the copper sites, mode of substrate binding and recognition by redox partner 1 1Edited by R. Huber . 10.1006/jmbi.1998.2007 . 1998 . Dodd . Fraser E. . Van Beeumen . Jos . Eady . Robert R. . Hasnain . S.Samar . Journal of Molecular Biology . 282 . 2 . 369–382 . 9735294 .
  10. The substrate-binding site in Cu nitrite reductase and its similarity to Zn carbonic anhydrase . 10.1038/nsb0495-287 . 1995 . Strange . Richard W. . Dodd . Fraser E. . Abraham . Zelda H.L. . Grossmann . J. Günter . Brüser . Thomas . Eady . Robert R. . Smith . Barry E. . Hasnain . S. Samar . Nature Structural & Molecular Biology . 2 . 4 . 287–292 . 7796265 . 21986822 .
  11. 10.1038/s41467-018-04114-x . The cysteine-reactive small molecule ebselen facilitates effective SOD1 maturation . 2018 . Capper . Michael J. . Wright . Gareth S. A. . Barbieri . Letizia . Luchinat . Enrico . Mercatelli . Eleonora . McAlary . Luke . Yerbury . Justin J. . o'Neill . Paul M. . Antonyuk . Svetlana V. . Banci . Lucia . Hasnain . S. Samar . Nature Communications . 9 . 1 . 1693 . 29703933 . 5923229 . 2018NatCo...9.1693C .
  12. 10.1038/ncomms2750 . Ligand binding and aggregation of pathogenic SOD1 . 2013 . Wright . Gareth S.A. . Antonyuk . Svetlana V. . Kershaw . Neil M. . Strange . Richard W. . Samar Hasnain . S. . Nature Communications . 4 . 1758 . 23612299 . 3644087 . 2013NatCo...4.1758W .
  13. 10.1073/pnas.0305143101 . Dimer destabilization in superoxide dismutase may result in disease-causing properties: Structures of motor neuron disease mutants . 2004 . Hough . Michael A. . Grossmann . J. Günter . Antonyuk . Svetlana V. . Strange . Richard W. . Doucette . Peter A. . Rodriguez . Jorge A. . Whitson . Lisa J. . Hart . P. John . Hayward . Lawrence J. . Valentine . Joan Selverstone . Hasnain . S. Samar . Proceedings of the National Academy of Sciences . 101 . 16 . 5976–5981 . 15056757 . 395908 . free .
  14. Amyloid-like filaments and water-filled nanotubes formed by SOD1 mutant proteins linked to familial ALS . 10.1038/nsb935 . 2003 . Elam . Jennifer Stine . Taylor . Alexander B. . Strange . Richard . Antonyuk . Svetlana . Doucette . Peter A. . Rodriguez . Jorge A. . Hasnain . S Samar . Hayward . Lawrence J. . Valentine . Joan Selverstone . Yeates . Todd O. . Hart . P John . Nature Structural & Molecular Biology . 10 . 6 . 461–467 . 12754496 . 22507679 .
  15. The Structure of Holo and Metal-deficient Wild-type Human Cu, Zn Superoxide Dismutase and its Relevance to Familial Amyotrophic Lateral Sclerosis . 10.1016/S0022-2836(03)00355-3 . 2003 . Strange . Richard W. . Antonyuk . Svetlana . Hough . Michael A. . Doucette . Peter A. . Rodriguez . Jorge A. . Hart . P.John . Hayward . Lawrence J. . Valentine . Joan S. . Hasnain . S.Samar . Journal of Molecular Biology . 328 . 4 . 877–891 . 12729761 .
  16. 10.1073/pnas.0809170106 . Crystal structure of human prion protein bound to a therapeutic antibody . 2009 . Antonyuk . S. V. . Trevitt . C. R. . Strange . R. W. . Jackson . G. S. . Sangar . D. . Batchelor . M. . Cooper . S. . Fraser . C. . Jones . S. . Georgiou . T. . Khalili-Shirazi . A. . Clarke . A. R. . Hasnain . S. S. . Collinge . J. . Proceedings of the National Academy of Sciences . 106 . 8 . 2554–2558 . 19204296 . 2637903 . 2009PNAS..106.2554A . free .
  17. Samantha. Price. 4 March 2014. TDP-43: A protein that lingers on... Web page. Proceedings of the National Academy of Sciences of the United States of America. Motor Neurone Disease Association. 111. 11. 4309–14. 2014PNAS..111.4309A. 10.1073/pnas.1317317111. 3964094. 24591609. 30 April 2014. free.
  18. Austin. J. A.. Wright. G. S. A.. Watanabe. S.. Grossmann. J. G.. Antonyuk. S. V.. Yamanaka. K.. Hasnain. S. S.. 2014. Disease causing mutants of TDP-43 nucleic acid binding domains are resistant to aggregation and have increased stability and half-life. Proceedings of the National Academy of Sciences. 111. 11. 4309–14. 2014PNAS..111.4309A. 10.1073/pnas.1317317111. 3964094. 24591609. free.
  19. Molecular structure of serum transferrin at 3.3-.ANG. Resolution . 10.1021/bi00415a061 . 1988 . Bailey . Susan . Evans . Robert W. . Garratt . Richard C. . Gorinsky . Beatrice . Hasnain . Samar . Horsburgh . Christopher . Jhoti . Harren . Lindley . Peter F. . Mydin . Assanah . Sarra . R. . Biochemistry . 27 . 15 . 5804–5812 . 3179277 .
  20. X-ray solution scattering reveals conformational changes upon iron uptake in lactoferrin, serum and ovo-transferrins . 10.1016/0022-2836(92)90402-6 . 1992 . Grossmann . J.Günter . Neu . Margarete . Pantos . Emmanuel . Schwab . Franz J. . Evans . Robert W. . Townes-Andrews . Elizabeth . Lindley . Peter F. . Appel . Helmut . Thies . Wolf-Gerolf . Hasnain . S.Samar . Journal of Molecular Biology . 225 . 3 . 811–819 . 1602483 .
  21. Constrained and restrained refinement in EXAFS data analysis with curved wave theory . 10.1021/bi00163a021 . 1992 . Binsted . Norman . Strange . Richard W. . Hasnain . S. Samar . Biochemistry . 31 . 48 . 12117–12125 . 1280998 . 45063154 .
  22. Vanadium K-edge x-ray absorption spectroscopy of bromoperoxidase from Ascophyllum nodosum . 10.1021/bi00445a062 . 1989 . Arber . J. M. . De Boer . E. . Garner . C. D. . Hasnain . S. S. . Wever . R. . Biochemistry . 28 . 19 . 7968–7973 . 2611224 .
  23. The CO bond angle of carboxymyoglobin determined by angular resolved XANES spectroscopy (1985) Bianconi, A., Congiu-Castellano, A., Durham, P. J., Hasnain S. S. and Phillips, S., Nature, 318, 685-687.
  24. XAFS study of the high-affinity copper-binding site of human PRP 91–231 and its low-resolution structure in solution 1 1Edited by I. A. Wilson . 10.1006/jmbi.2001.4795 . 2001 . Hasnain . S.Samar . Murphy . Loretta M. . Strange . Richard W. . Grossmann . J.Günter . Clarke . Anthony R. . Jackson . Graham S. . Collinge . John . Journal of Molecular Biology . 311 . 3 . 467–473 . 11493001 .
  25. An unprecedented dioxygen species revealed by serial femtosecond rotation crystallography in copper nitrite reductase . 10.1107/S2052252517016128 . 2018 . Halsted . Thomas P. . Yamashita . Keitaro . Hirata . Kunio . Ago . Hideo . Ueno . Go . Tosha . Takehiko . Eady . Robert R. . Antonyuk . Svetlana V. . Yamamoto . Masaki . Hasnain . S. Samar . IUCrJ . 5 . Pt 1 . 22–31 . 29354268 . 5755574 .
  26. 10.1098/rsta.2019.0147 . Synchrotron science in the UK: NINA, the SRS and Diamond . 2019 . Hasnain . S. Samar . Catlow . C. Richard A. . Philosophical Transactions of the Royal Society A: Mathematical, Physical and Engineering Sciences . 377 . 2147 . 31030660 . 6501895 . 2019RSPTA.37790147H .
  27. Vanadium K-edge X-ray absorption spectrum of the VFe protein of the vanadium nitrogenase of Azotobacter chroococcum  [(1987) Arber, J. M., Dobson, B. R., Eady, R. R., Stevens, P., Hasnain, S. S., Garner C. D. and Smith, B. E.</ref> and [[Neurodegeneration#Specific disorders|neurodegenerative diseases]][11] [12] [13] [14] [15] [16] [17] [18] and in structure-based drug discovery targeted towards neurodegenerative diseases and malaria.

    Hasnain has pioneered an approach to defining the structures of metalloproteins that combines not only X-ray crystallography[19] and solution X-ray scattering,[20] now used widely in the structural biology community, but also X-ray absorption fine structure (XAFS)[21] [22] [23] [24] and optical spectroscopies. More recently, he has used cryo-electron microscopy (cryo-EM), applied to a number of membrane proteins. The integration of spectroscopic methods with crystallography and the use of XFEL radiation for providing damage-free structures for redox proteins.[25]

    In 2019, Hasnain and Prof. Richard Catlow co-authored an article[26] giving personal accounts of how their work in the fields of structural molecular biology, materials and catalytic science developed and evolved using synchrotron techniques.

    References

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