Regular Papers

 

1994  
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2010

• J.A. Kyndt,, J.C. Fitch, S. Seibeck, B. Borucki, M.P. Heyn, T.E. Meyer, and M.A. Cusanovich
  Regulation of the Ppr histidine kinase by light-induced interaction between its photoactive yellow protein and bacteriophytochrome domains.
  Biochemistry 49, 1744-1754 (2010).
• C.P. Joshi, H. Otto, D. Hoersch, T. E. Meyer, M.A. Cusanovich, and M.P. Heyn
  Strong Hydrogen Bond between Glutamic Acid 46 and Chromophore Leads to the Intermediate Spectral Form and Excited State Proton Transfer in the Y42F Mutant of the Photoreceptor Photoactive Yellow Protein.
  Biochemistry 48, 9980-9993 (2009).
• D. Hoersch, H. Otto, M.A. Cusanovich, and M.P. Heyn
  Time-resolved spectroscopy of dye-labeled photoactive yellow protein suggests a pathway of light-induced structural changes in the N-terminal cap.
  Phys.Chem.Chem.Phys. 11, 5437-5444 (2009).
• B. Borucki, S. Seibeck, M.P. Heyn, and T. Lamparter
  Characterization of the covalent and noncovalent adducts of Agp1 phytochrome assembled with biliverdin and phycocyanobilin by circular dichroism and flash photolysis .
  Biochemistry 48, 6305-6317 (2009).
• D. Hoersch, H. Otto, M.A.Cusanovich, and M.P. Heyn
  Distinguishing chromophore structures of photocycle intermediates of the photoreceptor PYP by transient fluorescence and energy transfer.
  J.Phys.Chem. B 112, 9118-9125 (2008).
• D. Hoersch, H. Otto, I. Wallat and M.P. Heyn
  Monitoring the conformational changes of photoactivated rhodopsin from  microseconds to seconds by transient fluorescence spectroscopy.
  Biochemistry 47, 11518-11527 (2008).
• D. von Stetten, S. Seibeck, N. Michael, P. Scheerer, M.A. Mroginski, D.H. Murgida, N. Krauß, M.P. Heyn, P. Hildebrandt, B. Borucki, T. Lamparter
  Highly conserved residues D197 and H250 in Agp1 phytochrome control the proton affinity of the chromophore and Pfr formation.
  J. Biol. Chem. 282, 2116-2123 (2007). 
• J.A. Kyndt, S.N. Savvides, S. Memmi, M. Koch, J.C. Fitch, T.E. Meyer, M.P. Heyn, J.J. van Beeumen, and M.A. Cusanovich
  Structural role of tyrosine 98 in the photoactive yellow protein: effects on fluorescence, gateway and photocycle recovery.
  Biochemistry 46, 95-105 (2007).
• D. Hoersch, H. Otto, C. P. Joshi, B. Borucki, M. A. Cusanovich, M. P. Heyn
  Role of a conserved salt bridge between the PAS core and the N-terminal domain in the activation of the photoreceptor Photoactive Yellow Protein
  Biophys. J. 93, 1687-1699 (2007).
• S. Seibeck, B. Borucki, H. Otto, K. Inomata, H. Khawn, H. Kinoshita, N. Micheal, T. Lamparter, M. P. Heyn
  Locked 5Zs-biliverdin blocks the Meta-RA to Meta-RC transition in the functional cycle of bacteriophytochrome Agp1.
  FEBS Letters 581, 5425-5429 (2007).

• M.F. Brown, M.P. Heyn, C. Job, S. Kim, S. Moltke, K. Nakanishi, A.A. Nevzorov, A.V. Struts, G.F.J. Salgado, I. Wallat
  Solid-State ²H NMR Spectroscopy of Retinal Proteins in Aligned Membranes
  Biophys. Biochem. Acta 1768 , 2979-3000 (2007).
• B. Borucki
  Proton transfer in the photoreceptors phytochrome and Photoactive Yellow Protein. Photochem.
  Photobiol. Sci. 5, 553 - 566 (2006).
• C.P. Joshi, B. Borucki, H. Otto, T.E. Meyer,  M.A. Cusanovich and M.P. Heyn
  Photocycle and photoreversal of photoactive yellow protein at alkaline pH: kinetics, intermediates and equilibria.
  Biochemistry 45, 7057 - 7068 (2006).
• B. Borucki, C.P. Joshi, H. Otto, M.A. Cusanovich, and M.P. Heyn
  The transient accumulation of the signaling state of photoactive yellow protein is controlled by the external pH.
  Biophys. J. 91, 2991 - 3001 (2006).
• M. Birkholz, P. Zaumseil, M. Kittler, I. Wallat, and M.P. Heyn
  Structure of biomembrane - on - silicon derived from X-ray reflectometry.
  Materials Science and Engineering B 134, 125-129 (2006).
• B. Borucki, H. Otto, S. Seibeck and  M.P. Heyn
  Synchrotron radiation circular dichroism (SRCD) reveals structural changes in the photoreceptors phytochrome and photoactive yellow protein (PYP).
  In:"Research with synchrotron radiation", H.Dau, W.Kuch and R Puettner , eds,
  Shaker Verlag, 85-87 (2006).
• B. Borucki, H. Otto, T.E. Meyer, M.A. Cusanovich and M.P. Heyn
  Sensitive Circular Dichroism Marker for the Chromophore Environment of Photoactive Yellow Protein: Assignment of the 307 and 318 nm Bands to the n*-Transition of the Carbonyl.
  J. Phys. Chem. B109, 629-633( 2005).
• C.P.Joshi, B. Borucki, H. Otto, T.E. Meyer, M.A. Cusanovich and M.P. Heyn 
  Photoreversal kinetics of the I₁ and I₂ intermediates in the photocycle of photoactive yellow protein by double flash experiments with variable time delay.
  Biochemistry 44, 656-665 (2005).
• B. Borucki, D. von Stetten, S. Seibeck, T. Lamparter, N. Michael, M.A. Mroginski, H. Otto, D. H. Murgida, M.P. Heyn and P. Hildebrandt.
  Light-induced proton release of phytochrome is coupled to the transient deprotonation of the tetrapyrrole chromophore.
  J. Biol. Chem.  280, 34358-34364 (2005).
• B. Borucki, J.A. Kyndt, C.P. Joshi, H. Otto, T.E. Meyer, M.A. Cusanovich and M.P. Heyn
  Effect of salt and pH on the activation of photoactive yellow protein and gateway mutants Y98Q and Y98F.
  Biochemistry 44, 13650-13663 (2005).
• H. Otto, D. Hoersch, T.E. Meyer, M.A. Cusanovich and M.P. Heyn
  Time-Resolved Single Tryptophan Fluorescence in Photoactive Yellow Protein Monitors Changes in the Chromophore Structure during the Photocycle via Energy Transfer.
  Biochemistry 44, 16804-16816 (2005).
• B. Borucki, H. Otto and M.P. Heyn.
  Time-Resolved Linear Dichroism and Linear Birefringence of Bacteriorhodopsin at Alkaline pH: Identification of Two N Substates with Different Orientations of the Transition Dipole Moment.
  J. Phys. Chem. B 108, 2076-2086 (2004).
• T. Pöhlmann, R. A. Böckmann, H. Grubmüller, B. Uchanska-Ziegler, A. Ziegler and U. Alexiev.
  Differential peptide dynamics is linked to MHC polymorphism. 
  J. Biol. Chem. 279, 28197-28201 (2004).
• U. Alexiev, I. Rimke and T. Pöhlmann.
  Elucidation of the nature of the conformational changes of EF-interhelical loop in bacteriorhodopsin and of the helix VIII on the cytoplasmic surface of rhodopsin: A time-resolved fluorescence depolarization study.
  J. Mol. Biol. 328, 705-719 (2003).
• H.Otto, T. Lamparter, B. Borucki, J. Hughes and M.P. Heyn.
  Dimerization and Inter-Chromophore Distance of Cph1 Phytochrome from Synechocystis, as Monitored by Fluorescence Homo and Hetero Energy Transfer.
  Biochemistry 42, 5885-5895 (2003).
• B. Borucki, H. Otto, C.P. Joshi, C. Gasperi, M.A. Cusanovich, S. Devanathan, G. Tollin and M.P. Heyn.
  pH Dependence of the Photocycle Kinetics of the E46Q Mutant of Photoactive Yellow Protein: Protonation Equilibrium between I₁ and I₂ Intermediates, Chromophore Deprotonation by Hydroxyl Uptake, and Protonation Relaxation of the Dark State.
  Biochemistry 42, 8780-8790 (2003).
• B. Borucki, H. Otto, G. Rottwinkel, J. Hughes, M.P. Heyn and T. Lamparter.
  Mechanism of Cph1 Phytochrome Assembly from Stopped-Flow Kinetics and Circular Dichroism.
  Biochemistry 42, 13684-13697 (2003).
• B. Uchanska-Ziegler, U. Alexiev, R. Hillig, M. Hülsmeyer, T. Pöhlmann, W. Saenger, A. Volz and A. Ziegler.
  In "HLA 2002. the immunobiology of the human MHC" (Dupont B., Hansen J., eds.), IHWG Press, Seattle
• T. Mielke, C. Villa, P.C. Edwards, G.F.X. Schertler and M.P. Heyn.
  X-ray diffraction of heavy-atom labelled two-dimensional crystals of rhodopsin identifies the position of cysteine 140 in helix 3 and cysteine 316 in helix 8.
  Journal Mol. Biol. 316, 693-709 (2002).
• T. Mielke, U. Alexiev, M. Gläsel, H. Otto, and M.P. Heyn.
  Light-induced changes in the structure and accessibility of the cytoplasmic loops of rhodopsin in the activated M_II-state.
  Biochemistry 41, 7875-7884 (2002).
• B. Borucki, S. Devanathan, H. Otto, M.A. Cusanovich, G. Tollin and M.P. Heyn.
  Kinetics of proton uptake and dye binding by Photoactive Yellow Protein in wild-type, and in the E46Q and E46A mutants.
  Biochemistry, 41, 10026-10037(2002).
• R. A. Krebs, U. Alexiev, R. Parthasarathy, A.M. DeVita and M.S. Braiman
  Detection of fast light-activated H⁺ release and M intermediate formation from proteorhodopsin
  BioMed Central Physiology 2:5 (2002).
• J.J. van Thor, B. Borucki, W. Crielaard, H. Otto, T. Lamparter, J. Hughes, K.J. Hellingwerf and M.P. Heyn.
  Light-induced proton release and proton uptake reactions in the cyanobacterial phytochrome Cph1.
  Biochemistry 40, 11460-11471 (2001).
• U. Alexiev, R. Mollaaghababa, H.G. Khorana and M.P. Heyn.
  Evidence for Long Range Allosteric Interactions between the Extracellular and Cytoplasmic Parts of Bacteriorhodopsin from the Mutant R82A and its Second Site Revertant R82A/G231C.
  J. Biol. Chem. 275, 13431-13440 (2000).
• M.P. Heyn, B. Borucki and H. Otto.
  Chromophore reorientation during the photocycle of bacteriorhodopsin: experimental methods and functional significance.
  Biochim. Biophys. Acta 1460, 60-74 (2000).
• K. Heyne, J. Herbst, B. Dominguez-Herradon, U. Alexiev and R. Diller.
  Reaction Control in Bacteriorhodopsin: Impact of Arg82 and Asp85 on the fast Retinal Isomerization, Studied in the Second Site Revertant Arg82Ala/Gly231Cys and Various Purple and Blue Forms of Bacteriorhodopsin.
  J. Phys. Chem. B  104, 6053-6058 (2000).
• M.S. Hutson, U. Alexiev, S.V. Shilov, K.J. Wise, and M.S. Braiman.
  Evidence for a Perturbation of Arginine-82 in the Bacteriorhodopsin Photocycle from Time-Resolved Infrared Spectra.
  Biochemistry 39, 13189-13200 (2000).
• S. Moltke, I. Wallat, N. Sakai, K, Nakanishi, M.F. Brown and M.P. Heyn.
  The angles between the C₁-, C₅-, and C₉-methyl bonds of the retinylidene chromophore and the membrane normal increase in the M intermediate of bacteriorhodopsin: direct determination with solid-state ²H-NMR.
  Biochemistry 38, 11762-11772 (1999).
• A. Nevzorov, S. Moltke, M.P. Heyn and M.F. Brown.
  Solid-State NMR line shapes of uniaxiallly oriented immobile systems.
  J. Am. Chem. Soc. 121, 7636-7643 (1999).
• B. Borucki, H. Otto, and M.P. Heyn.
  Reorientation of the retinylidene chromophore in the K, L and M intermediates of bacteriorhodopsin from time-resolved linear dichroism: Resolving kinetically and spectrally overlapping intermediates of chromoproteins.
  J. Phys. Chem. B 103, 6371-6383 (1999).
• W. Behrens, U. Alexiev, R. Mollaaghababa, H.G. Khorana and M.P. Heyn.
  Structure of the interhelical loops and carboxyl terminus of bacteriorhodopsin by X-ray diffraction using site-directed heavy-atom labeling.
  Biochemistry 37, 10411-10419, (1998).
• W. Behrens, H. Otto, H.B. Stuhrmann and M.P. Heyn.
  Sulfur distribution in bacteriorhodopsin from multiple wavelength anomalous diffraction near the sulfur K-edge with synchrotron X-ray radiation.
  Biophys. J. 75, 255-263 (1998).
• B. Borucki, H. Otto and M.P. Heyn.
  Linear dichroism measurements on oriented purple membranes between parallel polarizers: contribution of linear birefringence and applications to chromophore isomerization.
  J. Phys. Chem. 102, 3821-3829 (1998).
• S. Moltke, A.A. Nevzorov, N. Sakai, I. Wallat, C. Job, K. Nakanishi, M.F. Brown and M.P. Heyn.
  Chromophore Orientation in Bacteriorhodopsin Determined from the Angular Dependence of Deuterium Nuclear Magnetic Resonance Spectra of Oriented Purple Membranes.
  Biochemistry 37,11821-11835 (1998).
• S. Dickopf, T. Mielke and M.P. Heyn.
  Kinetics of the Light-Induced Proton Translocation Associated with the pH-Dependent Formation of the Metarhodopsin I/II Equilibrium of Bovine Rhodopsin.
  Biochemistry 37,16888-16897 (1998).
• S. Dickopf and M.P. Heyn.
  Evidence for the first phase of the reprotonation switch of bacteriorhodopsin from time-resolved photovoltage and flashphotolysis experiments on the photoreversal of the M-intermediate.
  Biophys. J. 73, 3171-3181 (1997).
• A.S. Ulrich, I. Wallat, M.P. Heyn and A. Watts.
  Reorientation of the retinal chromophore in the M-intermediate of bacteriorhodopsin.
  Nature Structural Biology 2, 190-192 (1995).
• U. Alexiev, R. Mollaaghababa, P. Scherrer, H.G. Khorana and M.P. Heyn.
  Rapid long-range proton diffusion along the surface of the purple membrane and delayed proton transfer into the bulk.
  Proc. Natl. Acad. Sci. USA 92, 372-376 (1995).
• H. Otto, C. Zscherp, B. Borucki and M.P. Heyn.
  Time-resolved polarized absorption spectroscopy with isotropically excited oriented purple membranes: The orientation of the electronic transition dipole moment of the chromophore in the O-intermediate of bacteriorhodopsin.
  J. Phys. Chem. 99, 3847-3853 (1995).
• B. Watts, A.S. Sternberg, C.A. Ulrich, G. Whiteway, M. Seifert, P. Sami, P. Fisher, M.P. Heyn and I. Wallat.
  Bacteriorhodopsin: the effect of bilayer thickness on 2D-array formation and the structural re-alignment of retinal through the photocycle.
  Biophysical Chemistry 56, 41-46 (1995).
• U. Alexiev, P. Scherrer, T. Marti, H.G. Khorana and M.P. Heyn.
  Time-resolved surface charge change on the cytoplasmic side of bacteriorhodopsin during the decay of the M-intermediate.
  FEBS Letters 373, 81-84 (1995).
• S. Moltke and M.P. Heyn.
  Photovoltage kinetics of the acid-blue and acid-purple forms of bacteriorhodopsin: evidence for no net charge transfer.
  Biophys. J. 69, 2066-2073 (1995).
• S. Moltke, M.P. Krebs, R. Mollaaghababa, H.G. Khorana and M.P. Heyn.
  Intramolecular charge transfer in the bacteriorhodopsin mutants Asp85 -> Asn and Asp212 -> Asn: effects of pH and anions.
  Biophys. J. 69, 2074-2083 (1995).
• S. Moltke, U. Alexiev and M.P. Heyn.
  Kinetics of light-induced intramolecular charge transfer and proton release in bacteriorhodopsin.
  Israel J.Chem. 35, 401-414 (1995).
• S. Dickopf, U. Alexiev, M.P. Krebs, H. Otto, R. Mollaaghababa, H.G. Khorana and M.P. Heyn.
  Proton transport by a bacteriorhodopsin mutant, aspartic acid 85 -> asparagine, initiated in the unprotonated Schiff base state.
  Proc. Natl. Acad. Sci. USA 92, 11519-11523 (1995).
• U. Alexiev, T. Marti, M.P. Heyn, H.G. Khorana and P. Scherrer.
  Surface charge of bacteriorhodopsin detected with covalently bound pH-indicators at  selected extracellular and cytoplasmic sites.
  Biochemistry 33, 298-306 (1994).
• T. Hauß, G. Büldt, M.P. Heyn and N.A. Dencher.
  Light-induced isomerisation causes an increase in the chromophore tilt in the M-intermediate of bacteriorhodopsin: A neutron diffraction study.
  Proc. Natl. Acad. Sci. USA 91, 11854-11858 (1994).
• A.S. Ulrich, I. Wallat, A. Watts and M.P. Heyn.
  Distorted structure of the retinal chromophore in bacteriorhodopsin resolved by ²H-NMR.
  Biochemistry 33, 5370-5375 (1994).
• P. Scherrer, U. Alexiev, T. Marti, H.G. Khorana and M.P. Heyn.
  Covalently bound pH-indicator dyes at selected extracellular or cytoplasmic sites in bacteriorhodopsin. 1. Proton migration along the surface of bacteriorhodopsin micelles and its delayed transfer from surface to bulk.
  Biochemistry 33, 13684-13692 (1994).
• U. Alexiev, T. Marti, M.P. Heyn, H.G. Khorana and P. Scherrer.
  Covalently bound pH-indicator dyes at selected extracellular or cytoplasmic sites in bacteriorhodopsin. 2. Rotational orientation of helices D and E and kinetic correlation between M formation and proton release in bacteriorhodopsin micelles.
  Biochemistry 33, 13693-13699 (1994).