English Journal
- Enantioselective benzylic hydroxylation catalysed by P450 monooxygenases: characterisation of a P450cam mutant library and molecular modelling.
- Eichler A1, Gricman L2, Herter S3, Kelly P4, Turner N5, Pleiss J6, Flitsch S7.
- Chembiochem : a European journal of chemical biology.Chembiochem.2015 Dec 23. doi: 10.1002/cbic.201500536. [Epub ahead of print]
- Cytochrome P450 monooxygenases can catalyse the stereoselective C-H activation of a very broad range of substrates. Prediction and control of enantioselectivity of this enzyme class is of great interest for the synthesis of high value chiral molecules. Here we use a combination of molecular dynamics
- PMID 26698167
- Kinetic Consequences of Introducing a Proximal Selenocysteine Ligand into Cytochrome P450cam.
- Vandemeulebroucke A1, Aldag C1, Stiebritz MT1, Reiher M1, Hilvert D1.
- Biochemistry.Biochemistry.2015 Nov 10;54(44):6692-703. doi: 10.1021/acs.biochem.5b00939. Epub 2015 Oct 27.
- The structural, electronic, and catalytic properties of cytochrome P450cam are subtly altered when the cysteine that coordinates to the heme iron is replaced with a selenocysteine. To map the effects of the sulfur-to-selenium substitution on the individual steps of the catalytic cycle, we conducted
- PMID 26460790
- Comparison of PELDOR and RIDME for Distance Measurements between Nitroxides and Low-Spin Fe(III) Ions.
- Abdullin D1, Duthie F1, Meyer A1, Müller ES1, Hagelueken G1, Schiemann O1.
- The journal of physical chemistry. B.J Phys Chem B.2015 Oct 29;119(43):13534-42. doi: 10.1021/acs.jpcb.5b02118. Epub 2015 Jun 3.
- EPR-based nanometre distance measurements are becoming ever more important in structural biology. Usually the distance constraints are measured between two nitroxide spin labels. Yet, distance measurements between a metal center and spin labels enable, e.g., the localization of metal ions within the
- PMID 26000868
Japanese Journal
- Correlation between Activity and Molecular Structure around the Active Center of Cytochrome P450cam Conjugates
- JOURNAL OF CHEMICAL ENGINEERING OF JAPAN 49(5), 475-480, 2016
- NAID 130005152201
- Effect of length of molecular recognition moiety on enzymatic activity switching
- Journal of bioscience and bioengineering 116(4), 433-437, 2013-10
- NAID 110009675455
- Molecular recognition moiety and its target biomolecule interact in switching enzyme activity
- Journal of bioscience and bioengineering 115(6), 639-644, 2013-06-25
- NAID 110009614947
Related Links
- Cytochome P450 / P450cam / Activation of molecular oxygen / Acid-base catalyst / Site-directed mutagenesis / Artificial amino acids / Dioxygen-bond cleavage / Threonine / Hydrogen bonding / シトクロムP450 / 酸素活性化 / 酸 ...
- Measurement of the First and the Second Electron Transfer to P450cam Transfer of the first electron from reduced Pdx to P450cam was measured in carbon monoxide saturated 50 mM phosphate buffer, pH 7.5, containing 100 mM ...
Related Pictures
★リンクテーブル★
| リンク元 | 「camphor 5-monooxygenase」「CYP101」 |
| 拡張検索 | 「P450camタンパク質」 |
「camphor 5-monooxygenase」
「CYP101」
「P450camタンパク質」
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