tailieunhanh - Báo cáo Y học: Substrates modulate the rate-determining step for CO binding in cytochrome P450cam (CYP101) A high-pressure stopped-flow study

The high-pressure stopped-flow technique is applied to study the CO binding in cytochrome P450cam (P450cam) bound with homologous substrates (1R-camphor, camphane, norcamphor and norbornane) and in the substrate-free protein. The activation volume DV # of the CO on-rate is positive for P450cam bound with substrates that do not contain methyl groups. The kon rate constant for these substrate complexes is in the order of 3 · 106 M)1Æs)1. In contrast, P450cam complexed with substrates carrying methyl groups show a negative activation volume and a low kon rate constant of % 3 · 104 M)1Æs)1. . | Eur. J. Biochem. 269 2989-2996 2002 FEBS 2002 doi Substrates modulate the rate-determining step for CO binding in cytochrome P450cam CYP101 A high-pressure stopped-flow study Christiane Jung1 Nicole Bec2 and Reinhard Lange2 1 Max-Delbruck-Center for Molecular Medicine Protein Dynamics Laboratory Berlin Germany Anstitut National de la Sante et de la Recherche Medicale Unite 128 IFR24 Montpellier France The high-pressure stopped-flow technique is applied to study the CO binding in cytochrome P450cam P450cam bound with homologous substrates 1R-camphor camphane norcamphor and norbornane and in the substrate-free protein. The activation volume DV of the CO on-rate is positive for P450cam bound with substrates that do not contain methyl groups. The kon rate constant for these substrate complexes is in the order of 3 X 106 M-1-s-1. In contrast P450cam complexed with substrates carrying methyl groups show a negative activation volume and a low kon rate constant of w 3 X 104 M-1-s-1. By relating kon and DV with values for the compressibility and the influx rate of water for the heme pocket of the substrate complexes it is concluded that the positive activation volume is indicative for a loosely bound substrate that guarantees a high solvent accessibility for the heme pocket and a very compressible active site. In addition subconformers have been found for the substrate-free and camphane-bound protein which show different CO binding kinetics. Keywords high-pressure stopped-flow cytochrome P450 CO ligand binding protein dynamics. Cytochromes P450 represent a big superfamily of heme-type monooxygenases that catalyze the conversion of diverse substrates 1 . Besides the main route of the reaction cycle from the substrate to the product there are side reactions which lead to the production of cytotoxic oxygen species such as hydrogen peroxide or of water in the oxidase reaction. These so-called uncoupling processes have been observed in many .

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