J. Gutiérrez-Fernández*, H.-P. Hersleth* & M. Hammerstad*,
The crystal structure of mycothiol disulfide reductase Mtr provides mechanistic insight into the specific low-molecular weight thiol reductase activity of Actinobacteria. Acta Cryst. (2024), D80, 181-193. [Link]
M. Hammerstad*, A,K. Rugtveit, S. Dahlen, H.K. Andersen & H.-P. Hersleth*
Functional Diversity of Homologous Oxidoreductases—Tuning of Substrate Specificity by a FAD-Stacking Residue for Iron Acquisition and Flavodoxin Reduction. Antioxidants (2023), 12, 1224. [Link]
M. Shoor, I. Gudim, H.-P. Hersleth & M. Hammerstad*
Thioredoxin reductase from Bacillus cereus exhibits distinct reduction and NADPH-binding properties. FEBS Open Bio (2021), 11, 3019-3031. [Link]
M. Hammerstad* & H.-P. Hersleth*
Overview of structurally homologous flavoprotein oxidoreductases containing the low Mr thioredoxin reductase-like fold – A functionally diverse group.
For the special issue: Current Topics in Flavins and Flavoproteins Arch. Biochem. Biophys. (2021), 702, 108826. [Link]
M. Hammerstad*, I. Gudim & H.-P. Hersleth*
The Crystal Structures of Bacillithiol Disulfide Reductase Bdr (YpdA) Provide Structural and Functional Insight into a New Type of FAD-Containing NADPH-Dependent Oxidoreductase. Biochemistry (2020), 59, 4793-4798. [Link]
M. Hammerstad, Å.K. Røhr & H.-P. Hersleth*
A research-inspired biochemistry laboratory module - combining expression, purification, crystallization, structure solving, and characterization of a flavodoxin-like protein. Biochem. Mol. Biol. Educ. (2019), 47, 318-332. [Link]
I. Gudim*, M. Hammerstad, M. Lofstad & H.-P. Hersleth*
Characterization of different flavodoxin reductase-flavodoxin (FNR-Fld) interactions reveals an efficient FNR-Fld redox pair and identifies a novel FNR subclass. Biochemistry (2018), 57, 5427–5436. [Link]
I.K. Olsbu*, G. Zoppellaro, K.K. Andersson, J.-L. Boucher & H.-P. Hersleth*
Importance of Val567 on heme environment and substrate recognition of neuronal nitric oxide synthase. FEBS Open Bio (2018), 8, 1553-1566. [Link]
I. Gudim, M. Lofstad, W. van Beek & H.-P. Hersleth*
High-resolution crystal structures reveal a mixture of conformers of the Gly61-Asp62 peptide bond in an oxidised flavodoxin from Bacillus cereus. Protein Sci. (2018), 27, 1439-1449. [Link]
I. Gudim*, M. Lofstad, M. Hammerstad & H.-P. Hersleth*
Measurement of FNR-NrdI Interaction by Microscale Thermophoresis (MST). BioProtoc. (2017), 7, e2223. [Link]
M. Lofstad, I. Gudim, M. Hammerstad, Å.K. Røhr & H.-P. Hersleth*
Activation of the Class Ib Ribonucleotide Reductase by a Flavodoxin Reductase in Bacillus cereus. Biochemistry (2016), 55, 4998-5001. [Link]
S. Skråmo, H.-P. Hersleth*, M. Hammerstad, K.K. Andersson & Å.K. Røhr
Cloning, expression, purification, crystallisation and preliminary X-Ray diffraction analysis of a ferredoxin/flavodoxin-NADP(H) oxidoreductase (Bc0385) from Bacillus cereus. Acta Cryst. (2014), F70, 777-780. [Link]
M. Hammerstad, H.-P. Hersleth*, A.B. Tomter, Å.K. Røhr & K.K. Andersson
Crystal Structure of Bacillus cereus Class Ib Ribonucleotide Reductase Di-iron NrdF in Complex with NrdI. ACS Chem. Biol. (2014), 9, 526-537. [Link]
S. Rackwitz, I. Faus, H. Kelm, H.-J. Krüger, K.K. Andersson, H.-P. Hersleth, K. Achterhold, K. Schlage, H.-C. Wille, V. Schünemann & J.A. Wolny
A New Sample Environment for Cryogenic Nuclear Resonance Scattering Experiments on Single Crystals and Microsamples at P01, PETRA III. Hyperfine Interact.(2014), 226, 673-678. [Link]
X. Zhao, H.-P. Hersleth, J. Zhu, K.K. Andersson & R.S. Magliozzo
Access channel residues Ser315 and Asp137 in Mycobacterium tuberculosis catalase-peroxidase (KatG) control peroxidatic activation of the pro-drug isoniazid Chem. Commun.(2013), 49, 11650-11652. [Link]
M. Can, J. Krucinska, G. Zoppellaro, N.H. Andersen, J.E. Wedekind, H.-P. Hersleth*, K.K. Andersson & K.L. Bren.
Structural Characterization of Nitrosomonas europaea Cytochrome c-552 Variants with Marked Differences in Electronic Structure. ChemBioChem (2013), 14, 1828-1838. [Link]
A.B. Tomter, G. Zoppellaro, N.H. Andersen, H.-P. Hersleth, M. Hammerstad, Å.K. Røhr, G.K. Sandvik, K.R. Strand, G.E. Nilsson, C.B. Bell III, A.-L. Barra, E. Blasco, L. Le Pape, E.I. Solomon & K.K. Andersson
Ribonucleotide reductase class I with different radical generating clusters. Coord. Chem. Rev.(2013), 257, 3-26. [Link] Review.
C.B.F. Andersen, M. Torvund-Jensen, M.J. Nielsen, C.L. Pinto de Oliveira, H.-P. Hersleth, N.H. Andersen, J.S. Pedersen, G.R. Andersen & S.K. Moestrup.
Structure of the haptoglobin-haemoglobin complex. Nature(2012), 489, 456-459. [Link]
H.-P. Hersleth* & K.K. Andersson
How different oxidation states of crystalline myoglobin are influenced by X-rays.
For the special issue: Protein Structure and Function in the Crystalline State: from X-ray to Spectroscopy Biochim. Biophys. Acta, Proteins Proteomics (2011), 1814 , 785-796. [Link]
Å.K. Røhr, H.-P. Hersleth & K.K. Andersson
Tracking Flavin Conformations in Protein Crystal Structures with Raman Spectroscopy and QM/MM Calculations. Angew. Chem. Int. Ed. (2010), 49, 2324-2327. [Link]
K. Muffler, J.A. Wolny, H.-P. Hersleth, K.K. Andersson, K. Achterhold, R. Rüffer & V. Schünemann
Installation of an IR/Raman measuring station at the ESRF for simultaneous detection of vibrational and nuclear resonant scattering spectra. J. Phys.: Conf. Ser.(2010), 217, 012004 (4pp). [Link]
G. Zoppellaro, K.L. Bren, A.A. Esign, E. Harbitz, R. Kaur, H.-P. Hersleth, U. Ryde, L. Hederstedt & K.K. Andersson
Studies of Ferric 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(2009), 91, 1064-1082. [Link] Review.
H.-P. Hersleth, Y.-W. Hsiao, U. Ryde, C.H. Görbitz & K.K. Andersson The Influence of X-Rays on the Structural Studies of Peroxide-Derived Myoglobin Intermediates. Chem. Biodiv.(2008), 5, 2067-2089. [Link] Review.
H.-P. Hersleth, Y.-W. Hsiao, U. Ryde, C.H. Görbitz & K.K. Andersson
The crystal structure of peroxymyoglobin generated through cryoradiolytic reduction of myoglobin compound III during data collection. Biochem. J. (2008), 412, 257-264. [Link]
H.-P. Hersleth, A. Varnier, E. Harbitz, Å.K. Røhr, P.P. Schmidt, M. Sørlie, F.H. Cederkvist, S. Marchal, A.C.F. Gorren, B. Mayer, T. Uchida, V. Schünemann, T. Kitagawa, A.X. Trautwein, T. Shimizu, R. Lange, C.H. Görbitz & K.K. Andersson
Reactive complexes in myoglobin and nitric oxide synthase. Inorg. Chim. Acta (2008), 361, 831-843. [Link] Review.
H.-P. Hersleth, T. Uchida, Å.K. Røhr, T. Teschner, V. Schünemann, T. Kitagawa, A.X. Trautwein, C.H. Görbitz & K.K. Andersson
Crystallographic and spectroscopical studies of peroxide-derived myoglobin compound II and Occurence of protonated FeIV-O. J. Biol. Chem. (2007), 280, 23372-23386. [Link]
H.-P. Hersleth, U. Ryde, P. Rydberg, C.H. Görbitz & K.K. Andersson
Structures of the high-valent metal-ion haem-oxygen intermediates in peroxidases, oxygenases and catalases. J. Inorg. Biochem. (2006), 100, 460-476. [Link] Review.
K. Nilsson, H.-P. Hersleth, T.H. Rod, K.K. Andersson & U. Ryde
The Protonation Status of Compound II in Myoglobin, Studied by a Combination of Experimental Data and Quantum Chemical Calculations: Quantum Refinement. Biophys. J. (2004), 87, 3437-3447. [Link]
H.-P. Hersleth, B. Dalhus, C.H. Görbitz & K.K. Andersson
An iron hydroxide moiety in the 1.35 Å resolution structure of hydrogen peroxide derived myoglobin compund II at pH 5.2. J. Inorg. Biol. Chem. (2002), 7, 299-304. [Link]
C.H. Görbitz & H.-P. Hersleth
Selective solvent inclusion as a tool for mapping molecular properties in crystal structures - a diethylstilbestrol example. Acta Cryst. (2000), B56, 1094-1102. [Link]
C.H. Görbitz & H.-P. Hersleth
On the inclusion of solvent molecules in the crystal structure of organic compounds. Acta Cryst.(2000), B56, 526-534. [Link]