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Journal Abstract Search

181 related items for PubMed ID: 1991103

  • 1. Spectroscopic studies of myoglobin at low pH: heme ligation kinetics.
    Sage JT, Li PS, Champion PM.
    Biochemistry; 1991 Feb 05; 30(5):1237-47. PubMed ID: 1991103
    [Abstract] [Full Text] [Related]

  • 2. Functional implications of the proximal hydrogen-bonding network in myoglobin: a resonance Raman and kinetic study of Leu89, Ser92, His97, and F-helix swap mutants.
    Peterson ES, Friedman JM, Chien EY, Sligar SG.
    Biochemistry; 1998 Sep 01; 37(35):12301-19. PubMed ID: 9724545
    [Abstract] [Full Text] [Related]

  • 3. Spectroscopic studies of myoglobin at low pH: heme structure and ligation.
    Sage JT, Morikis D, Champion PM.
    Biochemistry; 1991 Feb 05; 30(5):1227-37. PubMed ID: 1991102
    [Abstract] [Full Text] [Related]

  • 4. A photolysis-triggered heme ligand switch in H93G myoglobin.
    Franzen S, Bailey J, Dyer RB, Woodruff WH, Hu RB, Thomas MR, Boxer SG.
    Biochemistry; 2001 May 01; 40(17):5299-305. PubMed ID: 11318654
    [Abstract] [Full Text] [Related]

  • 5. Carboxy Mb at pH 3. Time-resolved resonance Raman study at cryogenic temperatures.
    Iben IE, Cowen BR, Sanches R, Friedman JM.
    Biophys J; 1991 Apr 01; 59(4):908-19. PubMed ID: 2065191
    [Abstract] [Full Text] [Related]

  • 6. Metastable intermediates in myoglobin at low pH.
    Han S, Rousseau DL, Giacometti G, Brunori M.
    Proc Natl Acad Sci U S A; 1990 Jan 01; 87(1):205-9. PubMed ID: 2296580
    [Abstract] [Full Text] [Related]

  • 7. Crystal structures of CO-, deoxy- and met-myoglobins at various pH values.
    Yang F, Phillips GN.
    J Mol Biol; 1996 Mar 08; 256(4):762-74. PubMed ID: 8642596
    [Abstract] [Full Text] [Related]

  • 8. Investigations of photolysis and rebinding kinetics in myoglobin using proximal ligand replacements.
    Cao W, Ye X, Sjodin T, Christian JF, Demidov AA, Berezhna S, Wang W, Barrick D, Sage JT, Champion PM.
    Biochemistry; 2004 Aug 31; 43(34):11109-17. PubMed ID: 15323570
    [Abstract] [Full Text] [Related]

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  • 10. Resonance raman investigations of site-directed mutants of myoglobin: effects of distal histidine replacement.
    Morikis D, Champion PM, Springer BA, Sligar SG.
    Biochemistry; 1989 May 30; 28(11):4791-800. PubMed ID: 2765511
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  • 12. Proximal ligand motions in H93G myoglobin.
    Franzen S, Peterson ES, Brown D, Friedman JM, Thomas MR, Boxer SG.
    Eur J Biochem; 2002 Oct 30; 269(19):4879-86. PubMed ID: 12354119
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  • 14. Proximal and distal influences on ligand binding kinetics in microperoxidase and heme model compounds.
    Cao W, Ye X, Georgiev GY, Berezhna S, Sjodin T, Demidov AA, Wang W, Sage JT, Champion PM.
    Biochemistry; 2004 Jun 08; 43(22):7017-27. PubMed ID: 15170339
    [Abstract] [Full Text] [Related]

  • 15. Kinetic, structural, and spectroscopic identification of geminate states of myoglobin: a ligand binding site on the reaction pathway.
    Powers L, Chance B, Chance M, Campbell B, Friedman J, Khalid S, Kumar C, Naqui A, Reddy KS, Zhou Y.
    Biochemistry; 1987 Jul 28; 26(15):4785-96. PubMed ID: 3663626
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  • 17. Investigation of laser-induced long-lived states of photolyzed MbCO.
    Srajer V, Reinisch L, Champion PM.
    Biochemistry; 1991 May 21; 30(20):4886-95. PubMed ID: 2036357
    [Abstract] [Full Text] [Related]

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  • 19. Structural heterogeneity of the Fe(2+)-N epsilon (HisF8) bond in various hemoglobin and myoglobin derivatives probed by the Raman-active iron histidine stretching mode.
    Gilch H, Schweitzer-Stenner R, Dreybrodt W.
    Biophys J; 1993 Oct 21; 65(4):1470-85. PubMed ID: 8274641
    [Abstract] [Full Text] [Related]

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