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248 related items for PubMed ID: 15020591
1. Flavocytochrome P450 BM3 mutant A264E undergoes substrate-dependent formation of a novel heme iron ligand set. Girvan HM, Marshall KR, Lawson RJ, Leys D, Joyce MG, Clarkson J, Smith WE, Cheesman MR, Munro AW. J Biol Chem; 2004 May 28; 279(22):23274-86. PubMed ID: 15020591 [Abstract] [Full Text] [Related]
2. A single mutation in cytochrome P450 BM3 induces the conformational rearrangement seen upon substrate binding in the wild-type enzyme. Joyce MG, Girvan HM, Munro AW, Leys D. J Biol Chem; 2004 May 28; 279(22):23287-93. PubMed ID: 15020590 [Abstract] [Full Text] [Related]
3. Expression, purification, and characterization of Bacillus subtilis cytochromes P450 CYP102A2 and CYP102A3: flavocytochrome homologues of P450 BM3 from Bacillus megaterium. Gustafsson MC, Roitel O, Marshall KR, Noble MA, Chapman SK, Pessegueiro A, Fulco AJ, Cheesman MR, von Wachenfeldt C, Munro AW. Biochemistry; 2004 May 11; 43(18):5474-87. PubMed ID: 15122913 [Abstract] [Full Text] [Related]
4. Structural and spectroscopic characterization of P450 BM3 mutants with unprecedented P450 heme iron ligand sets. New heme ligation states influence conformational equilibria in P450 BM3. Girvan HM, Seward HE, Toogood HS, Cheesman MR, Leys D, Munro AW. J Biol Chem; 2007 Jan 05; 282(1):564-72. PubMed ID: 17077084 [Abstract] [Full Text] [Related]