1qmq: Difference between revisions
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==Overview== | ==Overview== | ||
The ability to detect, characterize, and manipulate specific biomolecules, in complex media is critical for understanding metabolic processes., Particularly important targets are oxygenases (cytochromes P450) involved, in drug metabolism and many disease states, including liver and kidney, dysfunction, neurological disorders, and cancer. We have found that Ru, photosensitizers linked to P450 substrates specifically recognize, submicromolar cytochrome P450(cam) in the presence of other heme proteins., In the P450:Ru-substrate conjugates, energy transfer to the heme, dramatically accelerates the Ru-luminescence decay. The crystal structure, of a P450(cam):Ru-adamantyl complex reveals access to the active center, via a channel whose depth (Ru-Fe distance is 21 A) is virtually the same, as .. | The ability to detect, characterize, and manipulate specific biomolecules, in complex media is critical for understanding metabolic processes., Particularly important targets are oxygenases (cytochromes P450) involved, in drug metabolism and many disease states, including liver and kidney, dysfunction, neurological disorders, and cancer. We have found that Ru, photosensitizers linked to P450 substrates specifically recognize, submicromolar cytochrome P450(cam) in the presence of other heme proteins., In the P450:Ru-substrate conjugates, energy transfer to the heme, dramatically accelerates the Ru-luminescence decay. The crystal structure, of a P450(cam):Ru-adamantyl complex reveals access to the active center, via a channel whose depth (Ru-Fe distance is 21 A) is virtually the same, as that extracted from an analysis of the energy-transfer kinetics., Suitably constructed libraries of sensitizer-linked substrates could be, employed to probe the steric and electronic properties of buried active, sites. | ||
==About this Structure== | ==About this Structure== | ||
1QMQ is a | 1QMQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida] with ACT, HEM and LRB as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Camphor_5-monooxygenase Camphor 5-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.15.1 1.14.15.1] Structure known Active Site: HEM. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QMQ OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: ru-substrate]] | [[Category: ru-substrate]] | ||
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Revision as of 16:24, 5 November 2007
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OPTICAL DETECTION OF CYTOCHROME P450 BY SENSITIZER-LINKED SUBSTRATES
OverviewOverview
The ability to detect, characterize, and manipulate specific biomolecules, in complex media is critical for understanding metabolic processes., Particularly important targets are oxygenases (cytochromes P450) involved, in drug metabolism and many disease states, including liver and kidney, dysfunction, neurological disorders, and cancer. We have found that Ru, photosensitizers linked to P450 substrates specifically recognize, submicromolar cytochrome P450(cam) in the presence of other heme proteins., In the P450:Ru-substrate conjugates, energy transfer to the heme, dramatically accelerates the Ru-luminescence decay. The crystal structure, of a P450(cam):Ru-adamantyl complex reveals access to the active center, via a channel whose depth (Ru-Fe distance is 21 A) is virtually the same, as that extracted from an analysis of the energy-transfer kinetics., Suitably constructed libraries of sensitizer-linked substrates could be, employed to probe the steric and electronic properties of buried active, sites.
About this StructureAbout this Structure
1QMQ is a Single protein structure of sequence from Pseudomonas putida with ACT, HEM and LRB as ligands. Active as Camphor 5-monooxygenase, with EC number 1.14.15.1 Structure known Active Site: HEM. Full crystallographic information is available from OCA.
ReferenceReference
Optical detection of cytochrome P450 by sensitizer-linked substrates., Dmochowski IJ, Crane BR, Wilker JJ, Winkler JR, Gray HB, Proc Natl Acad Sci U S A. 1999 Nov 9;96(23):12987-90. PMID:10557259
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