Professor Peter JF Henderson


Fulbright-Hays Scholar Wisconsin, USA; Royal Society (JSPS) Visiting Professor Jichi Idai, Japan; Commonwealth Senior Fellow, Guelph, Canada; Burroughs Wellcome Visiting Professor UNM USA; Leverhulme Senior Research Fellow, Leeds, UK; Visiting Research Fellow, Macquarie, Australia. Lecturer (Leicester) 1973-1975; Lecturer (Cambridge) 1975-1990; Reader (Cambridge) 1990-1992; Scientific Director European Membrane Protein (EMeP) consortium 2004-2008; Coordinator European Drug Initiative for Channels and Transporters (EDICT) 2008-2012.

Selected Publications

Hassan, K.A., Jackson, S.M., Penesyan, A., Patching, S.G., Tetu, S.G., Eijkelkamp, B.A., Brown, M.H., Hendersonn, P.J.F. and Ian. T. Paulsen, I.T. (2013) “Transcriptomic and biochemical analyses identify a novel family of chlorhexidine efflux proteins”. Proc Natl. Acad. Sci. USA. 110, 20254-20259.

Bettaney, K.E., Sukumar, P., Hussain, R. Siligardi, G., Henderson, P.J.F. and Patching, S.G. (2013) “A systematic approach to the amplified expression, functional characterization and purification of inositol transporters from Bacillus subtilis”. Molec. Memb. Biol. 30, 3-14.

Henderson, P.J.F. and Baldwin, S.A. (2012) “Bundles of insights into sugar transport proteins”. Nature 490, 348-350. 

Shimamura, T., Weyand, S., Beckstein, O., Rutherford, N.G., Hadden, J.M., Sharples, D., Sansom, , M.S.P., Iwata, S., Henderson, P.J.F. and Cameron, A.D. (2010) “Molecular basis of alternating access membrane transport by the sodium-hydantoin transporter Mhp1”. Science 328, 470-473.

Weyand, S., Shimamura, T., Yajima, S., Suzuki, S., Mirza O., Krusong, K., Carpenter, E.P., Rutherford, N.G., Hadden, J.M., O’Reilly, J., Ma, P., Saidijam, M., Patching, S.G., Hope, R.J., Norbertczak, H.T., Roach, P.C.J., Iwata, S., Henderson, P.J. F. and Cameron, A.D. (2008) Molecular basis of the alternating access model of membrane transport: structure of a nucleobase-cation-symport-1 family transporter. Science 322, 709 – 713.

Current Projects

A major goal is to determine the three-dimensional structure(s) of the proteins in the membrane using electron crystallography, X-ray crystallography and NMR. The proteins are being produced with cysteine, tryptophan and other residues engineered to facilitate these and other approaches. Working with Prof So Iwata and Dr Alex Cameron at Imperial College and the Diamond Synchrotron, the structure of an sodium-hydantoin transport protein has recently been determined in three conformations, open-out, occluded-with-substrate, and open-inwards (Figure 1). This enabled the structural basis of the alternating access mechanism of transport to be visualized for the first time. In addition genetical manipulation is used to determine which regions of each protein are involved in substrate recognition, cation recognition, inhibitor binding, translocation, Km, Vmax, Ki, etc. Individual amino acid residues are changed as informed by our databases of aligned transporter sequences.

 Most recently, collaborating with colleagues in Australia, we characterized a membrane protein involved in resistance to chlorhexidine, a widely used antiseptic.


Research interests

Membrane transport proteins, antibiotic resistance, molecular mechanisms of transport, developing physical methods to elucidate structure-activity relationships of membrane proteins.

Current major projects include:

  • Structure-activity relationship (SAR) of the Mhp1 transport protein
  • Application of mass spectrometry for elucidating SAR of membrane proteins
  • Efflux proteins for chlorhexidine in pathogenic bacteria
  • Application of NMR for elucidating SAR of membrane proteins

The laboratory is concerned with elucidating the structure-activity relationships of a wide range of membrane transport proteins found in bacteria. Included are uptake proteins for sugars and amino acids and efflux proteins for antibiotics from 'model' organisms like Escherichia coli and Bacillus subtilis, and from an increasing number of important pathogens such as Staphylococcus aureus, Helicobacter pylori, Acinetobacter baumannii, Brucella melitensis and others.

Our strategy is to transfer genes encoding transport proteins to suitable vectors for amplification of expression in E. coli. A number of the proteins are homologues to those found in man, so the bacteria provide a highly convenient model for illuminating the molecular mechanisms of mammalian transporters.

Proteins purified in 2-20 mg quantities are used for both 2D and 3D crystallisation trials and a variety of physical measurements - fluorimetry, NMR, EPR, CD, FTIR and mass spectrometry. Mutants and/or chimaeric proteins are also examined to locate substrate and inhibitor binding sites, elucidate the translocation process, facilitate structural studies, etc.

Outward- and inward- facing cavities in Mhp1.Figure 1. Outward- and inward- facing cavities in Mhp1. A slice through the Mhp1 structures, viewed parallel to the membrane is shown. (A) Mhp1 outward-open structure (substrate-free). (B) Mhp1 substrate-occluded with benzylhydantoin bound. (C) Mhp1 the open-inward cavity is shown. The benzylhydantoin is shown in cyan. Diagram taken from Shimamura et al. (2010).



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  • BSc 1965; PhD 1968, Bristol
  • MA 1975; ScD 1993, Cambridge

Professional memberships

  • Biochemical Society
  • Microbiology Society
  • Fellow of the Royal Society of Arts
  • Fellow of the Royal Society of Biology