[1]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=G1 / ATCC 17453;
PubMed=3003058 [NCBI, ExPASy, EBI, Israel, Japan]
Unger B.P.,
Gunsalus I.C.,
Sligar S.G.;
"Nucleotide sequence of the Pseudomonas putida cytochrome P-450cam gene and its expression in Escherichia coli.";
J. Biol. Chem. 261:1158-1163(1986).
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[2]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 386-415.
STRAIN=G1 / ATCC 17453;
PubMed=2613690 [NCBI, ExPASy, EBI, Israel, Japan]
Koga H.,
Yamaguchi E.,
Matsunaga K.,
Aramaki H.,
Horiuchi T.;
"Cloning and nucleotide sequences of NADH-putidaredoxin reductase gene (camA) and putidaredoxin gene (camB) involved in cytochrome P-450cam hydroxylase of Pseudomonas putida.";
J. Biochem. 106:831-836(1989).
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[3]
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PROTEIN SEQUENCE OF 2-415.
PubMed=7130171 [NCBI, ExPASy, EBI, Israel, Japan]
Haniu M.,
Armes L.G.,
Yasunobu K.T.,
Shastry B.A.,
Gunsalus I.C.;
"Amino acid sequence of the Pseudomonas putida cytochrome P-450. II. Cyanogen bromide peptides, acid cleavage peptides, and the complete sequence.";
J. Biol. Chem. 257:12664-12671(1982).
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[4]
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ABSORPTION SPECTROSCOPY.
DOI=10.1016/0003-9861(87)90642-4; PubMed=3813557 [NCBI, ExPASy, EBI, Israel, Japan]
Marden M.C.,
Hui Bon Hoa G.;
"P-450 binding to substrates camphor and linalool versus pressure.";
Arch. Biochem. Biophys. 253:100-107(1987).
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[5]
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FOURIER-TRANSFORM INFRARED SPECTROSCOPY.
Jung C.,
Marlow F.;
"Dynamic behavior of the active site structure in bacterial cytochrome P-450.";
Studia Biophys. 120:241-251(1987).
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[6]
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ABSORPTION SPECTROSCOPY, AND FLUORESCENCE SPECTROSCOPY.
DOI=10.1021/bi00428a035; PubMed=2578028 [NCBI, ExPASy, EBI, Israel, Japan]
Hui Bon Hoa G.,
Di Primo C.,
Dondaine I.,
Sligar S.G.,
Gunsalus I.C.,
Douzou P.;
"Conformational changes of cytochromes P-450cam and P-450lin induced by high pressure.";
Biochemistry 28:651-656(1989).
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[7]
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CIRCULAR DICHROISM ANALYSIS.
DOI=10.1016/0005-2728(92)90078-G; PubMed=1610873 [NCBI, ExPASy, EBI, Israel, Japan]
Nolting B.,
Jung C.,
Snatzke G.;
"Multichannel circular dichroism investigations of the structural stability of bacterial cytochrome P-450.";
Biochim. Biophys. Acta 1100:171-176(1992).
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[8]
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SUBSTRATE-PROTEIN INTERACTION.
DOI=10.1016/S0162-0134(02)00467-1; PubMed=12237225 [NCBI, ExPASy, EBI, Israel, Japan]
Deprez E.,
Gill E.,
Helms V.,
Wade R.,
Hui Bon Hoa G.;
"Specific and non-specific effects of potassium cations on substrate-protein interactions in cytochromes P450cam and P450lin.";
J. Inorg. Biochem. 91:597-606(2002).
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[9]
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X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
PubMed=4066706 [NCBI, ExPASy, EBI, Israel, Japan]
Poulos T.L.,
Finzel B.C.,
Gunsalus I.C.,
Wagner G.C.,
Kraut J.;
"The 2.6-A crystal structure of Pseudomonas putida cytochrome P-450.";
J. Biol. Chem. 260:16122-16130(1985).
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[10]
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X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
DOI=10.1016/S0014-5793(97)01135-6; PubMed=9357977 [NCBI, ExPASy, EBI, Israel, Japan]
Schlichting I.,
Jung C.,
Schulze H.;
"Crystal structure of cytochrome P-450cam complexed with the (1S)-camphor enantiomer.";
FEBS Lett. 415:253-257(1997).
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[11]
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X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
Di Gleria K.,
Nickerson D.P.,
Hill H.A.O.,
Wong L.-L.,
Fueloep V.;
"Covalent attachment of an electroactive sulfydryl reagent in the active site of cytochrome P450cam as revealed by the crystal structure of the modified protein.";
J. Am. Chem. Soc. 120:46-52(1998).
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[12]
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X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
DOI=10.1021/bi980189f; PubMed=9649301 [NCBI, ExPASy, EBI, Israel, Japan]
Vidakovic M.,
Sligar S.G.,
Li H.,
Poulos T.L.;
"Understanding the role of the essential Asp251 in cytochrome p450cam using site-directed mutagenesis, crystallography, and kinetic solvent isotope effect.";
Biochemistry 37:9211-9219(1998).
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[13]
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X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS).
DOI=10.1073/pnas.96.23.12987; PubMed=10557259 [NCBI, ExPASy, EBI, Israel, Japan]
Dmochowski I.J.,
Crane B.R.,
Wilker J.J.,
Winkler J.R.,
Gray H.B.;
"Optical detection of cytochrome P450 by sensitizer-linked substrates.";
Proc. Natl. Acad. Sci. U.S.A. 96:12987-12990(1999).
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[14]
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X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
DOI=10.1126/science.287.5458.1615; PubMed=10698731 [NCBI, ExPASy, EBI, Israel, Japan]
Schlichting I.,
Berendzen J.,
Chu K.,
Stock A.M.,
Maves S.A.,
Benson D.E.,
Sweet R.M.,
Ringe D.,
Petsko G.A.,
Sligar S.G.;
"The catalytic pathway of cytochrome p450cam at atomic resolution.";
Science 287:1615-1622(2000).
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[15]
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X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS).
PubMed=11098139 [NCBI, ExPASy, EBI, Israel, Japan]
Hishiki T.,
Shimada H.,
Nagano S.,
Egawa T.,
Kanamori Y.,
Makino R.,
Park S.-Y.,
Adachi S.,
Shiro Y.,
Ishimura Y.;
"X-ray crystal structure and catalytic properties of Thr252Ile mutant of cytochrome P450cam: roles of Thr252 and water in the active center.";
J. Biochem. 128:965-974(2000).
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[16]
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X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
DOI=10.1021/bi002225s; PubMed=11258878 [NCBI, ExPASy, EBI, Israel, Japan]
Lee D.-S.,
Park S.-Y.,
Yamane K.,
Obayashi E.,
Hori H.,
Shiro Y.;
"Structural characterization of n-butyl-isocyanide complexes of cytochromes P450nor and P450cam.";
Biochemistry 40:2669-2677(2001).
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[17]
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X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
DOI=10.1073/pnas.221297998; PubMed=11606730 [NCBI, ExPASy, EBI, Israel, Japan]
Dunn A.R.,
Dmochowski I.J.,
Bilwes A.M.,
Gray H.B.,
Crane B.R.;
"Probing the open state of cytochrome P450cam with ruthenium-linker substrates.";
Proc. Natl. Acad. Sci. U.S.A. 98:12420-12425(2001).
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[18]
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X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
DOI=10.1016/S0003-9861(02)00555-6; PubMed=12464241 [NCBI, ExPASy, EBI, Israel, Japan]
Fedorov R.,
Ghosh D.K.,
Schlichting I.;
"Crystal structures of cyanide complexes of P450cam and the oxygenase domain of inducible nitric oxide synthase -- structural models of the short-lived oxygen complexes.";
Arch. Biochem. Biophys. 409:25-31(2003).
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[19]
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STRUCTURE BY NMR.
DOI=10.1016/S0014-5793(97)00995-2; PubMed=9315686 [NCBI, ExPASy, EBI, Israel, Japan]
Mouro C.,
Bondon A.,
Simmoneaux G.,
Jung C.;
"1H-NMR study of diamagnetic cytochrome P450cam: assignment of heme resonances and substrate dependance of one cysteinate beta proton.";
FEBS Lett. 414:203-208(1997).
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