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Journal Abstract Search


257 related items for PubMed ID: 18001135

  • 1. Alteration of P450 distal pocket solvent leads to impaired proton delivery and changes in heme geometry.
    Makris TM, von Koenig K, Schlichting I, Sligar SG.
    Biochemistry; 2007 Dec 11; 46(49):14129-40. PubMed ID: 18001135
    [Abstract] [Full Text] [Related]

  • 2. Understanding the role of the essential Asp251 in cytochrome p450cam using site-directed mutagenesis, crystallography, and kinetic solvent isotope effect.
    Vidakovic M, Sligar SG, Li H, Poulos TL.
    Biochemistry; 1998 Jun 30; 37(26):9211-9. PubMed ID: 9649301
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  • 3. Cryoreduction EPR and 13C, 19F ENDOR study of substrate-bound substates and solvent kinetic isotope effects in the catalytic cycle of cytochrome P450cam and its T252A mutant.
    Kim SH, Yang TC, Perera R, Jin S, Bryson TA, Sono M, Davydov R, Dawson JH, Hoffman BM.
    Dalton Trans; 2005 Nov 07; (21):3464-9. PubMed ID: 16234926
    [Abstract] [Full Text] [Related]

  • 4. A role of the heme-7-propionate side chain in cytochrome P450cam as a gate for regulating the access of water molecules to the substrate-binding site.
    Hayashi T, Harada K, Sakurai K, Shimada H, Hirota S.
    J Am Chem Soc; 2009 Feb 04; 131(4):1398-400. PubMed ID: 19133773
    [Abstract] [Full Text] [Related]

  • 5. Density functional theory applied to a difference in pathways taken by the enzymes cytochrome P450 and superoxide reductase: spin States of ferric hydroperoxo intermediates and hydrogen bonds from water.
    Surawatanawong P, Tye JW, Hall MB.
    Inorg Chem; 2010 Jan 04; 49(1):188-98. PubMed ID: 19968237
    [Abstract] [Full Text] [Related]

  • 6. Structural evidence for a functionally relevant second camphor binding site in P450cam: model for substrate entry into a P450 active site.
    Yao H, McCullough CR, Costache AD, Pullela PK, Sem DS.
    Proteins; 2007 Oct 01; 69(1):125-38. PubMed ID: 17598143
    [Abstract] [Full Text] [Related]

  • 7. Stabilizing bound O2 in myoglobin by valine68 (E11) to asparagine substitution.
    Krzywda S, Murshudov GN, Brzozowski AM, Jaskolski M, Scott EE, Klizas SA, Gibson QH, Olson JS, Wilkinson AJ.
    Biochemistry; 1998 Nov 10; 37(45):15896-907. PubMed ID: 9843395
    [Abstract] [Full Text] [Related]

  • 8. Mechanism of O2 activation by cytochrome P450cam studied by isotope effects and transient state kinetics.
    Purdy MM, Koo LS, de Montellano PR, Klinman JP.
    Biochemistry; 2006 Dec 26; 45(51):15793-806. PubMed ID: 17176102
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  • 11. QM/MM study of the second proton transfer in the catalytic cycle of the D251N mutant of cytochrome P450cam.
    Altarsha M, Wang D, Benighaus T, Kumar D, Thiel W.
    J Phys Chem B; 2009 Jul 16; 113(28):9577-88. PubMed ID: 19537775
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  • 12. Infrared spectroscopic and mutational studies on putidaredoxin-induced conformational changes in ferrous CO-P450cam.
    Nagano S, Shimada H, Tarumi A, Hishiki T, Kimata-Ariga Y, Egawa T, Suematsu M, Park SY, Adachi S, Shiro Y, Ishimura Y.
    Biochemistry; 2003 Dec 16; 42(49):14507-14. PubMed ID: 14661963
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  • 15. Resonance Raman characterization of the peroxo and hydroperoxo intermediates in cytochrome P450.
    Denisov IG, Mak PJ, Makris TM, Sligar SG, Kincaid JR.
    J Phys Chem A; 2008 Dec 18; 112(50):13172-9. PubMed ID: 18630867
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  • 16. Cytochrome P450CAM enzymatic catalysis cycle: a quantum mechanics/molecular mechanics study.
    Guallar V, Friesner RA.
    J Am Chem Soc; 2004 Jul 14; 126(27):8501-8. PubMed ID: 15238007
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  • 17. Substrate modulation of the properties and reactivity of the oxy-ferrous and hydroperoxo-ferric intermediates of cytochrome P450cam as shown by cryoreduction-EPR/ENDOR spectroscopy.
    Davydov R, Perera R, Jin S, Yang TC, Bryson TA, Sono M, Dawson JH, Hoffman BM.
    J Am Chem Soc; 2005 Feb 09; 127(5):1403-13. PubMed ID: 15686372
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  • 18. Roles of the proximal hydrogen bonding network in cytochrome P450cam-catalyzed oxygenation.
    Yoshioka S, Tosha T, Takahashi S, Ishimori K, Hori H, Morishima I.
    J Am Chem Soc; 2002 Dec 11; 124(49):14571-9. PubMed ID: 12465966
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  • 19. Structural changes in cytochrome P-450cam effected by the binding of the enantiomers (1R)-camphor and (1S)-camphor.
    Schulze H, Hoa GH, Helms V, Wade RC, Jung C.
    Biochemistry; 1996 Nov 12; 35(45):14127-38. PubMed ID: 8916898
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  • 20. Speeding up proton transfer in a fast enzyme: kinetic and crystallographic studies on the effect of hydrophobic amino acid substitutions in the active site of human carbonic anhydrase II.
    Fisher SZ, Tu C, Bhatt D, Govindasamy L, Agbandje-McKenna M, McKenna R, Silverman DN.
    Biochemistry; 2007 Mar 27; 46(12):3803-13. PubMed ID: 17330962
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