Education
Ph.D, Department of Chemistry, University of Oslo, Norway, 2007
Current position
Senior Lecturer/Principal Investigator, Department of Biosciences and Department of Chemistry, University of Oslo, Norway
Publications
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Lofstad, M., Gudim, I., Hammerstad, M., Rohr, A. K. and Hersleth, H. P. (2016). Activation of the Class Ib Ribonucleotide Reductase by a Flavodoxin Reductase in Bacillus cereus. Biochemistry 55(36): 4998-5001.
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Skramo, S., Hersleth, H. P., Hammerstad, M., Andersson, K. K. and Rohr, A. K. (2014). Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of a ferredoxin/flavodoxin-NADP(H) oxidoreductase (Bc0385) from Bacillus cereus. Acta Crystallogr F Struct Biol Commun 70(Pt 6): 777-780.
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Hammerstad, M., Hersleth, H. P., Tomter, A. B., Rohr, A. K. and Andersson, K. K. (2014). Crystal structure of Bacillus cereus class Ib ribonucleotide reductase di-iron NrdF in complex with NrdI. ACS Chem Biol 9(2): 526-537.
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Rackwitz, S., Faus, I., Schmitz, M., Kelm, H., Krüger, H. J., Andersson, K. K., Hersleth, H. P., Achterhold, K., Schlage, K., Wille, H. C., Schünemann, V. and Wolny, J. A. (2014). A New Sample Enviroment for Cryogenic Nuclear Resonance Scattering experiments on Single Crystals and Microsamples at P01, PETRA III. Hyperfine Interactions 226: 673-678.
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Zhao, X., Hersleth, H. P., Zhu, J., Andersson, K. K. and Magliozzo, R. S. (2013). Access channel residues Ser315 and Asp137 in Mycobacterium tuberculosis catalase-peroxidase (KatG) control peroxidatic activation of the pro-drug isoniazid. Chem Commun (Camb) 49(99): 11650-11652.
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Can, M., Krucinska, J., Zoppellaro, G., Andersen, N. H., Wedekind, J. E., Hersleth, H. P., Andersson, K. K. and Bren, K. L. (2013). Structural characterization of nitrosomonas europaea cytochrome c-552 variants with marked differences in electronic structure. Chembiochem 14(14): 1828-1838.
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Tomter, A. B., Zoppellaro, G., Andersen, N. H., Hersleth, H. P., Hammerstad, M., Røhr, Å. K., Sandvik, G. K., Strand, K. R., Nilsson, G. E., Bell III, C. B., Barra, A. L., Blasco, E., Le Pape, L., Solomon, E. I. and Andersson, K. K. (2013). Ribonucleotide reductase class I with different radical generating clusters. Coord. Chem. Rev. 257(1): 3-26.
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Andersen, C. B., Torvund-Jensen, M., Nielsen, M. J., de Oliveira, C. L., Hersleth, H. P., Andersen, N. H., Pedersen, J. S., Andersen, G. R. and Moestrup, S. K. (2012). Structure of the haptoglobin-haemoglobin complex. Nature 489(7416): 456-459.
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Hersleth, H. P. and Andersson, K. K. (2011). How different oxidation states of crystalline myoglobin are influenced by X-rays. Biochim Biophys Acta 1814(6): 785-796.
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Rohr, A. K., Hersleth, H. P. and Andersson, K. K. (2010). Tracking flavin conformations in protein crystal structures with Raman spectroscopy and QM/MM calculations. Angew Chem Int Ed Engl 49(13): 2324-2327.
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Muffler, K., Wolny, J. A., Hersleth, H. P., Andersson, K. K., Achterhold, K., Rüffer, R. and Schünemann, V. (2010). Installation of an IR/Raman measuring station at the ESRF for simultaneous detection of vibrational and nuclear resonant scattering spectra. J. Phys.: Conf. Ser. 217: 012004, 4pp.
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Zoppellaro, G., Bren, K. L., Ensign, A. A., Harbitz, E., Kaur, R., Hersleth, H. P., Ryde, U., Hederstedt, L. and Andersson, K. K. (2009). Review: studies of ferric heme proteins with highly anisotropic/highly axial low spin (S = 1/2) electron paramagnetic resonance signals with bis-histidine and histidine-methionine axial iron coordination. Biopolymers 91(12): 1064-1082.
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Hersleth, H. P., Hsiao, Y. W., Ryde, U., Gorbitz, C. H. and Andersson, K. K. (2008). The influence of X-rays on the structural studies of peroxide-derived myoglobin intermediates. Chem Biodivers 5(10): 2067-2089.
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Hersleth, H. P., Hsiao, Y. W., Ryde, U., Gorbitz, C. H. and Andersson, K. K. (2008). The crystal structure of peroxymyoglobin generated through cryoradiolytic reduction of myoglobin compound III during data collection. Biochem J 412(2): 257-264.
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Hersleth, H. P., Varnier, A., Harbitz, E., Røhr, Å. K., Schmidt, P. P., Sørlie, M., Cederkvist, F. H., Marchal, S., Gorren, A. C. F., Mayer, B., Uchida, T., Schünemann, V., Kitagawa, T., Trautwein, A. X., Shimizu, T., Lange, R., Görbitz, C. H. and Andersson, K. K. (2008). Reactive complexes in myoglobin and nitric oxide synthase. Inorg. Chim. Acta 361(4): 831-843.
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Hersleth, H. P., Uchida, T., Rohr, A. K., Teschner, T., Schunemann, V., Kitagawa, T., Trautwein, A. X., Gorbitz, C. H. and Andersson, K. K. (2007). Crystallographic and spectroscopic studies of peroxide-derived myoglobin compound II and occurrence of protonated FeIV O. J Biol Chem 282(32): 23372-23386.
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Hersleth, H. P., Ryde, U., Rydberg, P., Gorbitz, C. H. and Andersson, K. K. (2006). Structures of the high-valent metal-ion haem-oxygen intermediates in peroxidases, oxygenases and catalases. J Inorg Biochem 100(4): 460-476.
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Nilsson, K., Hersleth, H. P., Rod, T. H., Andersson, K. K. and Ryde, U. (2004). The protonation status of compound II in myoglobin, studied by a combination of experimental data and quantum chemical calculations: quantum refinement. Biophys J 87(5): 3437-3447.
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Hersleth, H. P., Dalhus, B., Gorbitz, C. H. and Andersson, K. K. (2002). An iron hydroxide moiety in the 1.35 A resolution structure of hydrogen peroxide derived myoglobin compound II at pH 5.2. J Biol Inorg Chem 7(3): 299-304.
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Gorbitz, C. H. and Hersleth, H. P. (2000). Selective solvent inclusion as a tool for mapping molecular properties in crystal structures: a diethylstilbestrol example. Acta Crystallogr B 56 ( Pt 6): 1094-1102.
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Gorbitz, C. H. and Hersleth, H. P. (2000). On the inclusion of solvent molecules in the crystal structures of organic compounds. Acta Crystallogr B 56 (Pt 3): 526-534.