R W Hendler

Summary

Affiliation: National Institutes of Health
Country: USA

Publications

  1. doi request reprint Further studies with isolated absolute infrared spectra of bacteriorhodopsin photocycle intermediates: conformational changes and possible role of a new proton-binding center
    Richard W Hendler
    National Institutes of Health, Laboratory of Cell Biology, National Heart, Lung, and Blood Institute, Bethesda, MD 20892, USA
    Appl Spectrosc 67:73-85. 2013
  2. doi request reprint Infrared and visible absolute and difference spectra of bacteriorhodopsin photocycle intermediates
    Richard W Hendler
    Laboratory of Cell Biology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892, USA
    Appl Spectrosc 65:1029-45. 2011
  3. ncbi request reprint Importance of lipids for bacteriorhodopsin structure, photocycle, and function
    R W Hendler
    Laboratory of Cell Biology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland, 20892, USA
    Biochemistry (Mosc) 66:1311-4. 2001
  4. pmc Electrogenic proton-pumping capabilities of the m-fast and m-slow photocycles of bacteriorhodopsin
    Richard W Hendler
    Laboratory of Cell Biology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892, USA
    Biochemistry 47:5396-405. 2008
  5. ncbi request reprint Interconversions among four M-intermediates in the bacteriorhodopsin photocycle
    Richard W Hendler
    Laboratory of Cell Biology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892 0510, USA
    Eur J Biochem 270:3518-24. 2003
  6. pmc The ability of actinic light to modify the bacteriorhodopsin photocycle revisited: heterogeneity vs photocooperativity
    Richard W Hendler
    Laboratory of Cell Biology, National Heart, Lung, and Blood Institute, and Mathematical and Statistical Computing Laboratory, Center for Information Technology, National Institutes of Health, Bethesda, Maryland 20892, USA
    Biochemistry 47:5406-16. 2008
  7. pmc Simultaneous measurements of fast optical and proton current kinetics in the bacteriorhodopsin photocycle using an enhanced spectrophotometer
    John W Kakareka
    Division of Computational Bioscience, Center for Information Technology, Bethesda, Maryland, 20892, United States
    J Biochem Biophys Methods 70:1116-23. 2008
  8. ncbi request reprint An apparent general solution for the kinetic models of the bacteriorhodopsin photocycles
    Richard W Hendler
    Laboratory of Cell Biology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892, USA
    J Phys Chem B 109:16515-28. 2005
  9. ncbi request reprint Purple membrane lipid control of bacteriorhodopsin conformational flexibility and photocycle activity
    Richard W Hendler
    Laboratory of Cell Biology, National Heart, Lung, and Blood Institute, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892 0510, USA
    Eur J Biochem 270:1920-5. 2003
  10. pmc Direct measurement of the initial and early ratios of proton extrusion to oxygen uptake accompanying cytochrome c oxidation by rat liver mitoplasts
    R W Hendler
    Laboratory of Cell Biology, National Heart, Lung, and Blood Institute, Bethesda, Maryland 20892
    Biophys J 53:205-13. 1988

Collaborators

  • John W Kakareka
  • Paul D Smith
  • Thomas J Pohida

Detail Information

Publications11

  1. doi request reprint Further studies with isolated absolute infrared spectra of bacteriorhodopsin photocycle intermediates: conformational changes and possible role of a new proton-binding center
    Richard W Hendler
    National Institutes of Health, Laboratory of Cell Biology, National Heart, Lung, and Blood Institute, Bethesda, MD 20892, USA
    Appl Spectrosc 67:73-85. 2013
    ..Below, we present evidence that supports this interpretation and propose a possible role for this new component...
  2. doi request reprint Infrared and visible absolute and difference spectra of bacteriorhodopsin photocycle intermediates
    Richard W Hendler
    Laboratory of Cell Biology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892, USA
    Appl Spectrosc 65:1029-45. 2011
    ..Notably, the Arg82 deprotonation occurs exclusively in the M(F) pathway of the parallel cycles model of the photocycle...
  3. ncbi request reprint Importance of lipids for bacteriorhodopsin structure, photocycle, and function
    R W Hendler
    Laboratory of Cell Biology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland, 20892, USA
    Biochemistry (Mosc) 66:1311-4. 2001
    ..Participation of a peripheral acidic amino acid in the overall expression of fast-decaying M is also discussed. Initial studies suggest that the acidic amino acid may be Asp36 and/or Asp38...
  4. pmc Electrogenic proton-pumping capabilities of the m-fast and m-slow photocycles of bacteriorhodopsin
    Richard W Hendler
    Laboratory of Cell Biology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892, USA
    Biochemistry 47:5396-405. 2008
    ..The optical and electrical data in these studies were collected simultaneously by a newly designed and built spectrometer which is described separately...
  5. ncbi request reprint Interconversions among four M-intermediates in the bacteriorhodopsin photocycle
    Richard W Hendler
    Laboratory of Cell Biology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892 0510, USA
    Eur J Biochem 270:3518-24. 2003
    ..Interconversions of the 2-ms and 5-ms species of the wild-type are accomplished by pH-changes. The potential significance of these findings is discussed...
  6. pmc The ability of actinic light to modify the bacteriorhodopsin photocycle revisited: heterogeneity vs photocooperativity
    Richard W Hendler
    Laboratory of Cell Biology, National Heart, Lung, and Blood Institute, and Mathematical and Statistical Computing Laboratory, Center for Information Technology, National Institutes of Health, Bethesda, Maryland 20892, USA
    Biochemistry 47:5406-16. 2008
    ..On the basis of new information presented here, it seems that a heterogeneous branched model is more likely than one with separate linear sequences...
  7. pmc Simultaneous measurements of fast optical and proton current kinetics in the bacteriorhodopsin photocycle using an enhanced spectrophotometer
    John W Kakareka
    Division of Computational Bioscience, Center for Information Technology, Bethesda, Maryland, 20892, United States
    J Biochem Biophys Methods 70:1116-23. 2008
    ..Matching the time constants for the two processes indicates which molecular transformations are associated with major proton movements...
  8. ncbi request reprint An apparent general solution for the kinetic models of the bacteriorhodopsin photocycles
    Richard W Hendler
    Laboratory of Cell Biology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892, USA
    J Phys Chem B 109:16515-28. 2005
    ....
  9. ncbi request reprint Purple membrane lipid control of bacteriorhodopsin conformational flexibility and photocycle activity
    Richard W Hendler
    Laboratory of Cell Biology, National Heart, Lung, and Blood Institute, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892 0510, USA
    Eur J Biochem 270:1920-5. 2003
    ....
  10. pmc Direct measurement of the initial and early ratios of proton extrusion to oxygen uptake accompanying cytochrome c oxidation by rat liver mitoplasts
    R W Hendler
    Laboratory of Cell Biology, National Heart, Lung, and Blood Institute, Bethesda, Maryland 20892
    Biophys J 53:205-13. 1988
    ..Implications of the previous (Setty et al., 1986) and current studies on defining "mechanistic" H+/O ratios are discussed...
  11. pmc High voltage redox properties of cytochrome c oxidase
    R W Hendler
    Laboratory of Cell Biology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892
    Biophys J 58:957-67. 1990
    ..1990. Biophys. J. 57:1125-1140) two different forms, which are distinguishable by their redox potentials, spectra, and reactivity with CO...