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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 [Abstract] [Full Text] [Related]
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6. Cytochrome P450cam: crystallography, oxygen activation, and electron transfer. Poulos TL, Raag R. FASEB J; 1992 Jan 06; 6(2):674-9. PubMed ID: 1537455 [Abstract] [Full Text] [Related]
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9. [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 Jun 30; 26(6):1251-62. PubMed ID: 1491671 [Abstract] [Full Text] [Related]
10. Controlling the regiospecificity and coupling of cytochrome P450cam: T185F mutant increases coupling and abolishes 3-hydroxynorcamphor product. Paulsen MD, Filipovic D, Sligar SG, Ornstein RL. Protein Sci; 1993 Mar 30; 2(3):357-65. PubMed ID: 8453374 [Abstract] [Full Text] [Related]
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