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Journal Abstract Search

413 related items for PubMed ID: 9370469

  • 21. Resonance Raman enhancement of phenyl ring vibrational modes in phenyl iron complex of myoglobin.
    Liu HH, Lin SH, Yu NT.
    Biophys J; 1990 Apr; 57(4):851-6. PubMed ID: 2344468
    [Abstract] [Full Text] [Related]

  • 22. Role of heme iron coordination and protein structure in the dynamics and geminate rebinding of nitric oxide to the H93G myoglobin mutant: implications for nitric oxide sensors.
    Negrerie M, Kruglik SG, Lambry JC, Vos MH, Martin JL, Franzen S.
    J Biol Chem; 2006 Apr 14; 281(15):10389-98. PubMed ID: 16476730
    [Abstract] [Full Text] [Related]

  • 23. Ligand binding to synthetic mutant myoglobin (His-E7----Gly): role of the distal histidine.
    Braunstein D, Ansari A, Berendzen J, Cowen BR, Egeberg KD, Frauenfelder H, Hong MK, Ormos P, Sauke TB, Scholl R.
    Proc Natl Acad Sci U S A; 1988 Nov 14; 85(22):8497-501. PubMed ID: 3186740
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  • 24. Temperature-dependent studies of NO recombination to heme and heme proteins.
    Ionascu D, Gruia F, Ye X, Yu A, Rosca F, Beck C, Demidov A, Olson JS, Champion PM.
    J Am Chem Soc; 2005 Dec 07; 127(48):16921-34. PubMed ID: 16316238
    [Abstract] [Full Text] [Related]

  • 25. 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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  • 28. On the origin of heme absorption band shifts and associated protein structural relaxation in myoglobin following flash photolysis.
    Franzen S, Boxer SG.
    J Biol Chem; 1997 Apr 11; 272(15):9655-60. PubMed ID: 9092494
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  • 31. Resonance Raman investigation of the effects of copper binding to iron-mesoporphyrin.histidine-rich glycoprotein complexes.
    Larsen RW, Nunez DJ, Morgan WT, Muhoberac BB, Ondrias MR.
    Biophys J; 1992 Apr 11; 61(4):1007-17. PubMed ID: 1581496
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  • 32. Modulation of protein function by exogenous ligands in protein cavities: CO binding to a myoglobin cavity mutant containing unnatural proximal ligands.
    Decatur SM, DePillis GD, Boxer SG.
    Biochemistry; 1996 Apr 02; 35(13):3925-32. PubMed ID: 8672423
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  • 33. 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
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  • 35. 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
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  • 37. Electrostatic modification of the active site of myoglobin: characterization of the proximal Ser92Asp variant.
    Lloyd E, Burk DL, Ferrer JC, Maurus R, Doran J, Carey PR, Brayer GD, Mauk AG.
    Biochemistry; 1996 Sep 10; 35(36):11901-12. PubMed ID: 8794773
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  • 38. Ligand binding to heme proteins. VI. Interconversion of taxonomic substates in carbonmonoxymyoglobin.
    Johnson JB, Lamb DC, Frauenfelder H, Müller JD, McMahon B, Nienhaus GU, Young RD.
    Biophys J; 1996 Sep 10; 71(3):1563-73. PubMed ID: 8874030
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  • 39. Modification of the distal histidyl imidazole in myoglobin to N-tetrazole-substituted imidazole and its effects on the heme environmental structure and ligand binding properties.
    Adachi S, Morishima I.
    Biochemistry; 1992 Sep 15; 31(36):8613-8. PubMed ID: 1390645
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  • 40. 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]

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