L358P Mutation on Cytochrome P450cam Simulates Structural Changes upon Putidaredoxin Binding
نویسندگان
چکیده
منابع مشابه
Substrate binding induces structural changes in cytochrome P450cam
The binding of (+)-camphor to cytochrome P450cam (P450cam) expels a cluster of waters at the active site, raising the redox potential of the haem to an extent that allows reduction by the electron-transfer system. This binding was reported to involve no significant structural changes in the protein. Here, two ferric P450cam structures partially complexed with (+)-camphor were determined by X-ra...
متن کاملDetection of a high-barrier conformational change in the active site of cytochrome P450cam upon binding of putidaredoxin.
The orientation of the substrate camphor in the active site of reduced CO-bound cytochrome P450cam (CYP101) as a function of reduced putidaredoxin (Pdxr) addition has been examined by NMR using perdeuterated CYP101 and perdeuterated Pdx as well as isotopically labeled d-camphor. This permits the 1H resonances of CYP101-bound camphor to be observed without interference from the signals of CYP101...
متن کاملCombined QM/MM Studies of Binding Effect of Cytochrome P450cam to Putidaredoxin
Combined QM/MM calculations of an activesite of Cytochrome P450cam have been performed, before and after a binding process of Cytochrome P450cam to Putidaredoxin. The calculations have been carried out for two coordination spheres of the heme active-site of Cytochrome P450cam, namely a 5-coordinated, and a 6coordinated system of this protein having a water molecule as a 6th ligand. An experimen...
متن کاملThe Role of Water Molecules in the Association of Cytochrome P450cam with Putidaredoxin
We have investigated the osmotic pressure dependence of the association between ferric cytochrome P450cam and putidaredoxin (Pdx) to gain an insight into the role of water molecules in the P450cam-reduced Pdx complexation amenable to physiological electron transfer. The association constant was evaluated from the electron transfer rates from reduced Pdx to P450cam. The natural logarithm of the ...
متن کاملDouble electron-electron resonance shows cytochrome P450cam undergoes a conformational change in solution upon binding substrate.
Although cytochrome P450cam from Pseudomonas putida, the archetype for all heme monooxygenases, has long been known to have a closed active site, recent reports show that the enzyme can also be crystallized in at least two clusters of open conformations. This suggests that the enzyme may undergo significant conformational changes during substrate binding and catalytic turnover. However, these c...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2004
ISSN: 0021-9258
DOI: 10.1074/jbc.m404216200