Cytochrome P450: Structure, Mechanism, and Biochemistry - download pdf or read online

By Paul R. Ortiz de Montellano

ISBN-10: 3319121073

ISBN-13: 9783319121079

ISBN-10: 3319121081

ISBN-13: 9783319121086

This authoritative Fourth variation summarizes the advances of the earlier decade about the constitution, mechanism, and biochemistry of cytochrome P450 enzymes, with adequate insurance of previous paintings to make each one bankruptcy a finished assessment of the sphere. 13 chapters are divided into distinct volumes, the 1st overlaying the basics of cytochrome P450 biochemistry, in addition to the microbial, plant, and bug structures, and the second one solely targeting mammalian systems.

Volume 1 starts with an exploration of the biophysics and mechanistic enzymology of cytochrome P450 enzymes, with a dialogue of the constructions of P450 enzymes and their electron donor companions, the mechanisms of oxygen activation and substrate oxidation, and the methods and nature of cytochrome P450 inhibition. extra chapters talk about the character and roles of cytochrome P450 enzymes in microbes, vegetation and bugs, and an 8th bankruptcy is a survey of the capability software of P450 enzymes in biotechnology. the 1st bankruptcy of quantity 2 examines the jobs of P450 enzymes in mammals, usually people. 4 extra chapters then care for the genetic and hormonal law of P450 enzymes and their particular roles within the processing of sterols and lipids. Cytochrome P450: constitution, Mechanism, and Biochemistry is a key source for scientists, professors, and scholars drawn to fields as varied as biochemistry, chemistry, biophysics, molecular biology, pharmacology and toxicology.

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Cytochrome P450: Structure, Mechanism, and Biochemistry - download pdf or read online

This authoritative Fourth version summarizes the advances of the earlier decade in regards to the constitution, mechanism, and biochemistry of cytochrome P450 enzymes, with adequate assurance of prior paintings to make each one bankruptcy a complete overview of the sphere. 13 chapters are divided into designated volumes, the 1st masking the basics of cytochrome P450 biochemistry, in addition to the microbial, plant, and bug platforms, and the second one completely targeting mammalian platforms.

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Extra info for Cytochrome P450: Structure, Mechanism, and Biochemistry

Example text

Johnson that the FMN domain docks on the proximal surface of the P450, which was expected, based on complementary electrostatic surfaces and mutagenesis studies The linker connecting the heme and FMN domains had been proteolyzed during crystallization, thus raising the possibility that the structure is an artifact of crystallization Further experiments were carried out to test the functional validity of the model Residues found at the interface were probed by mutagenesis [123] Replacing Leu104 of P450BM3 with a Cys (Fig 120) at the interface should not alter binding or electron transfer because replacing Leu with a smaller side chain should not cause any steric problems in forming the proper complex However, covalent modification of the mutant Cys104 side chain with a large fluorophore should interfere with electron transfer For these studies, laser flash photolysis was used wherein a laser flash photoreduced a potent reductant, deazariboflavin, which in turn reduces the FMN in the complex The reduced FMN semiquinone then reduces the P450 heme As predicted, mutation of Leu104 to Cys had no effect, while chemical modification of Cys104 dramatically decreased the FMN-to-heme electron transfer rate, thus Fig.

In addition to the binding site for the FMN prosthetic group, this domain contains residues mediating binding of and electron transfer to acceptors such as cyt c and P450.

L. Poulos and E. F. Johnson that the FMN domain docks on the proximal surface of the P450, which was expected, based on complementary electrostatic surfaces and mutagenesis studies The linker connecting the heme and FMN domains had been proteolyzed during crystallization, thus raising the possibility that the structure is an artifact of crystallization Further experiments were carried out to test the functional validity of the model Residues found at the interface were probed by mutagenesis [123] Replacing Leu104 of P450BM3 with a Cys (Fig 120) at the interface should not alter binding or electron transfer because replacing Leu with a smaller side chain should not cause any steric problems in forming the proper complex However, covalent modification of the mutant Cys104 side chain with a large fluorophore should interfere with electron transfer For these studies, laser flash photolysis was used wherein a laser flash photoreduced a potent reductant, deazariboflavin, which in turn reduces the FMN in the complex The reduced FMN semiquinone then reduces the P450 heme As predicted, mutation of Leu104 to Cys had no effect, while chemical modification of Cys104 dramatically decreased the FMN-to-heme electron transfer rate, thus Fig.

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Cytochrome P450: Structure, Mechanism, and Biochemistry by Paul R. Ortiz de Montellano


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