Spring-loading the active site of cytochrome P450cam
نویسندگان
چکیده
منابع مشابه
Active-site hydration and water diffusion in cytochrome P450cam: a highly dynamic process.
Long-timescale molecular dynamics simulations (300 ns) are performed on both the apo- (i.e., camphor-free) and camphor-bound cytochrome P450cam (CYP101). Water diffusion into and out of the protein active site is observed without biased sampling methods. During the course of the molecular dynamics simulation, an average of 6.4 water molecules is observed in the camphor-binding site of the apo f...
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 کاملIntramolecular electron transfer in a cytochrome P450cam system with a site-specific branched structure.
Cytochrome P450 (P450) is an attractive oxygenase due to the diverse catalytic reactions and the broad substrate specificity. Class I P450s require an excess concentration (more than 10 times) of iron-sulfur proteins, which transfer electrons to P450s, to attain the maximum catalytic activity and this requirement is a critical bottleneck for practical applications. Here, we show a site-specific...
متن کاملCharacterizing the proton loading site in cytochrome c oxidase.
Cytochrome c oxidase (CcO) uses the energy released by reduction of O2 to H2O to drive eight charges from the high pH to low pH side of the membrane, increasing the electrochemical gradient. Four electrons and protons are used for chemistry, while four more protons are pumped. Proton pumping requires that residues on a pathway change proton affinity through the reaction cycle to load and then r...
متن کاملDelicate conformational balance of the redox enzyme cytochrome P450cam.
The energy landscapes of proteins are highly complex and can be influenced by changes in physical and chemical conditions under which the protein is studied. The redox enzyme cytochrome P450cam undergoes a multistep catalytic cycle wherein two electrons are transferred to the heme group and the enzyme visits several conformational states. Using paramagnetic NMR spectroscopy with a lanthanoid ta...
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ژورنال
عنوان ژورنال: Metallomics
سال: 2011
ISSN: 1756-5901,1756-591X
DOI: 10.1039/c0mt00065e