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Structure paper

TitleProbing the open state of cytochrome P450cam with ruthenium-linker substrates.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 98, Page 12420-12425, Year 2001
Publish dateSep 28, 2001 (structure data deposition date)
AuthorsDunn, A.R. / Dmochowski, I.J. / Bilwes, A.M. / Gray, H.B. / Crane, B.R.
External linksProc. Natl. Acad. Sci. USA / PubMed:11606730
MethodsX-ray diffraction
Resolution1.65 Å
Structure data

PDB-1k2o:
Cytochrome P450Cam with Bound BIS(2,2'-BIPYRIDINE)-(5-METHYL-2-2'-BIPYRIDINE)-C2-ADAMANTANE RUTHENIUM (II)
Method: X-RAY DIFFRACTION / Resolution: 1.65 Å

Chemicals

ChemComp-CAC:
CACODYLATE ION

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

ChemComp-RFA:
DELTA-BIS(2,2'-BIPYRIDINE)-(5-METHYL-2-2'-BIPYRIDINE)-C2-ADAMANTANE RUTHENIUM (II)

ChemComp-RFB:
LAMBDA-BIS(2,2'-BIPYRIDINE)-(5-METHYL-2-2'-BIPYRIDINE)-C2-ADAMANTANE RUTHENIUM (II)

ChemComp-HOH:
WATER

Source
  • pseudomonas putida (bacteria)
KeywordsOXIDOREDUCTASE / P450 / monooxygenase / electron transfer / energy transfer / fluorinated aromatics / biphenyl / adamantane / ruthenium channel / substrate-binding

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