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Journal Abstract Search

1005 related items for PubMed ID: 9724545

  • 1. 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
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  • 2. 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 01; 65(4):1470-85. PubMed ID: 8274641
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  • 3. Spectroscopic study of Ser92 mutants of human myoglobin: hydrogen bonding effect of Ser92 to proximal His93 on structure and property of myoglobin.
    Shiro Y, Iizuka T, Marubayashi K, Ogura T, Kitagawa T, Balasubramanian S, Boxer SG.
    Biochemistry; 1994 Dec 20; 33(50):14986-92. PubMed ID: 7999755
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  • 4. Conformational change and histidine control of heme chemistry in cytochrome c peroxidase: resonance Raman evidence from Leu-52 and Gly-181 mutants of cytochrome c peroxidase.
    Smulevich G, Miller MA, Kraut J, Spiro TG.
    Biochemistry; 1991 Oct 01; 30(39):9546-58. PubMed ID: 1654102
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  • 6. 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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  • 8. A possible allosteric communication pathway identified through a resonance Raman study of four beta37 mutants of human hemoglobin A.
    Peterson ES, Friedman JM.
    Biochemistry; 1998 Mar 31; 37(13):4346-57. PubMed ID: 9521755
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  • 9. 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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  • 10. Spectroscopic effects of polarity and hydration in the distal heme pocket of deoxymyoglobin.
    Christian JF, Unno M, Sage JT, Champion PM, Chien E, Sligar SG.
    Biochemistry; 1997 Sep 16; 36(37):11198-204. PubMed ID: 9287162
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  • 11. Inversion of axial coordination in myoglobin to create a "proximal" ligand binding pocket.
    Uno T, Sakamoto R, Tomisugi Y, Ishikawa Y, Wilkinson AJ.
    Biochemistry; 2003 Sep 02; 42(34):10191-9. PubMed ID: 12939147
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  • 12. Resonance Raman studies indicate a unique heme active site in prostaglandin H synthase.
    Lou BS, Snyder JK, Marshall P, Wang JS, Wu G, Kulmacz RJ, Tsai AL, Wang J.
    Biochemistry; 2000 Oct 10; 39(40):12424-34. PubMed ID: 11015223
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  • 14. 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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  • 17. 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 10; 61(4):1007-17. PubMed ID: 1581496
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  • 18. The Fe(2+)-His(F8) Raman band shape of deoxymyoglobin reveals taxonomic conformational substates of the proximal linkage.
    Schott J, Dreybrodt W, Schweitzer-Stenner R.
    Biophys J; 2001 Sep 10; 81(3):1624-31. PubMed ID: 11509375
    [Abstract] [Full Text] [Related]

  • 19. Structural characterization of the proximal and distal histidine environment of cytoglobin and neuroglobin.
    Sawai H, Makino M, Mizutani Y, Ohta T, Sugimoto H, Uno T, Kawada N, Yoshizato K, Kitagawa T, Shiro Y.
    Biochemistry; 2005 Oct 11; 44(40):13257-65. PubMed ID: 16201751
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  • 20. Structure and ligand binding properties of myoglobins reconstituted with monodepropionated heme: functional role of each heme propionate side chain.
    Harada K, Makino M, Sugimoto H, Hirota S, Matsuo T, Shiro Y, Hisaeda Y, Hayashi T.
    Biochemistry; 2007 Aug 21; 46(33):9406-16. PubMed ID: 17636874
    [Abstract] [Full Text] [Related]

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