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Journal Abstract Search

474 related items for PubMed ID: 19133773

  • 1. 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
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  • 2. 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
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  • 3. How do substrates enter and products exit the buried active site of cytochrome P450cam? 1. Random expulsion molecular dynamics investigation of ligand access channels and mechanisms.
    Lüdemann SK, Lounnas V, Wade RC.
    J Mol Biol; 2000 Nov 10; 303(5):797-811. PubMed ID: 11061976
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  • 4. Molecular recognition in (+)-alpha-pinene oxidation by cytochrome P450cam.
    Bell SG, Chen X, Sowden RJ, Xu F, Williams JN, Wong LL, Rao Z.
    J Am Chem Soc; 2003 Jan 22; 125(3):705-14. PubMed ID: 12526670
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  • 7. Dynamics of protein-bound water in the heme domain of P450BM3 studied by high-pressure spectroscopy: comparison with P450cam and P450 2B4.
    Davydov DR, Hui Bon Hoa G, Peterson JA.
    Biochemistry; 1999 Jan 12; 38(2):751-61. PubMed ID: 9888815
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  • 9. Evaluation of the functional role of the heme-6-propionate side chain in cytochrome P450cam.
    Harada K, Sakurai K, Ikemura K, Ogura T, Hirota S, Shimada H, Hayashi T.
    J Am Chem Soc; 2008 Jan 16; 130(2):432-3. PubMed ID: 18088124
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  • 10. Effect of alcohols on binding of camphor to cytochrome P450cam: spectroscopic and stopped flow transient kinetic studies.
    Murugan R, Mazumdar S.
    Arch Biochem Biophys; 2006 Nov 15; 455(2):154-62. PubMed ID: 17049478
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  • 11. [Electron-conformational interactions at the active site of reduced bacterial cytochrome P450cam induced by a substrate and analysis of the electron structure of heme].
    Sharonov IuA.
    Mol Biol (Mosk); 1992 Nov 15; 26(6):1251-62. PubMed ID: 1491671
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  • 13. Structures of the siroheme- and Fe4S4-containing active center of sulfite reductase in different states of oxidation: heme activation via reduction-gated exogenous ligand exchange.
    Crane BR, Siegel LM, Getzoff ED.
    Biochemistry; 1997 Oct 07; 36(40):12101-19. PubMed ID: 9315848
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  • 14. 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
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  • 15. 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. Improved binding of cytochrome P450cam substrate analogues designed to fill extra space in the substrate binding pocket.
    Helms V, Deprez E, Gill E, Barret C, Hui Bon Hoa G, Wade RC.
    Biochemistry; 1996 Feb 06; 35(5):1485-99. PubMed ID: 8634279
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  • 18. Structure-activity correlations in pentachlorobenzene oxidation by engineered cytochrome P450cam.
    Xu F, Bell SG, Rao Z, Wong LL.
    Protein Eng Des Sel; 2007 Oct 06; 20(10):473-80. PubMed ID: 17962225
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  • 19. 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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  • 20. 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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