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Structure paper

TitleStructural and spectroscopic characterization of P450 BM3 mutants with unprecedented P450 heme iron ligand sets. New heme ligation states influence conformational equilibria in P450 BM3.
Journal, issue, pagesJ. Biol. Chem., Vol. 282, Page 564-572, Year 2007
Publish dateSep 29, 2006 (structure data deposition date)
AuthorsGirvan, H.M. / Seward, H.E. / Toogood, H.S. / Cheesman, M.R. / Leys, D. / Munro, A.W.
External linksJ. Biol. Chem. / PubMed:17077084
MethodsX-ray diffraction
Resolution1.2 - 2.4 Å
Structure data

PDB-2ij2:
Atomic structure of the heme domain of flavocytochrome P450-BM3
Method: X-RAY DIFFRACTION / Resolution: 1.2 Å

PDB-2ij3:
Structure of the A264H mutant of cytochrome P450 BM3
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-2ij4:
Structure of the A264K mutant of cytochrome P450 BM3
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

Chemicals

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

ChemComp-HOH:
WATER

Source
  • bacillus megaterium (bacteria)
KeywordsOXIDOREDUCTASE / Cytochrome P450 / P450BM3 / monoxygenase / heme binding protein / atomic resolution / heme ligation / histidine ligation / P450 BM3 / lysine heme ligation

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