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001			81380
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007			cr nn 008mamaa
008			150522s2015 gw | s |||| 0|eng d
020			_a9783319160092
024	7		_a10.1007/978-3-319-16009-2 _2doi
050		4	_aQP671.C83 _bM666 2015
082	0	4	_a610
245	1	0	_aMonooxygenase, Peroxidase and Peroxygenase Properties and Mechanisms of Cytochrome P450 _cedited by Eugene G. Hrycay, Stelvio M. Bandiera.
260			_aCham, Switzerland _bSpringer _c2015
300			_a1 recurso en línea (XV, 368 p.) _b150 ilustraciones, 59 ilustraciones en color
336			_aTexto (visual) _btxt _2rdacontent
337			_aelectrónico _bc _2rdamedia
338			_arecurso electrónico _bcr _2rdacarrier
490	1		_aAdvances in Experimental Medicine and Biology _x0065-2598 _v851
505	0		_aForeword -- 1. Monooxygenase, Peroxidase and Peroxygenase Properties and Reaction Mechanisms of Cytochrome P450 Enzymes -- 2. Oxidizing Intermediates in P450 Catalysis: A Case for Multiple Oxidants -- 3. Current Approaches for Investigating and Predicting Cytochrome P450 3A4-Ligand Interactions -- 4. Acyl-Carbon Bond Cleaving Cytochrome P450 Enzymes: CYP17A1, CYP19A1 and CYP51A1 -- 5. Regioselective Versatility of Monooxygenase Reactions Catalyzed by CYP2B6 and CYP3A4: Examples With Single Substrates -- 6. Cytochrome P450 Enzymes in the Bioactivation of Polyunsaturated Fatty Acids and their Role in Cardiovascular Disease -- 7. Monooxygenation of Small Hydrocarbons Catalyzed by Bacterial Cytochrome P450s -- 8. Use of Chemical Auxiliaries to Control P450 Enzymes for Predictable Oxidations at Unactivated C-H Bonds of Substrates,- 9. Cytochrome P450 Enzymes and Electrochemistry: Crosstalk with Electrodes as Redox Partners and Electron Sources -- 10. Mechanistic Basis of Electron Transfer to Cytochromes P450 by Natural Redox Partners and Artificial Donor Constructs -- 11. Biological Diversity of Cytochrome P450 Redox Partner Proteins -- 12. Cytochrome P450cin (CYP176A1) -- 13. Fungal Unspecific Peroxygenases: Heme-Thiolate Proteins that Combine Peroxidase and Cytochrome P450 Properties.
520			_aThis book describes in 13 chapters mechanisms of P450 used to monooxygenate substrates via the NAD(P)H/O2 pathway using its peroxidase and peroxygenase functions. P450 also utilizes peroxides, peracids, periodate and iodosobenzene to oxygenate substrates via the shunt pathway. Also described are mechanisms used in the oxidation of pharmaceuticals by CYP3A4; acyl- carbon cleavage by CYP17A1, CYP19A1 and CYP51A1; metabolism of tetrabromodiphenyl ethers and bile acids by CYP2B6 and CYP3A4; metabolism of Ï{uDDA0}and Ï{uDCE0}polyunsaturated fatty acids; H2O2-mediated peroxygenation of substrates using substrate misrecognition; P450 oxidative reactions using electrochemical methods; electron transfer to P450 by redox proteins; hydroxylation of 1,8-cineole by P450cin; and peroxygenation by unspecific peroxygenases using H2O2. The topics covered are relevant to P450 researchers, professors and students from a variety of disciplines ranging from pharmacology, toxicology and microbiology to chemistry.
710	2		_aSpringerLink (Online service) _0Local _9106996
942			_2lcc _cLE
988			_aEBOOK, EBSPRINGER
650	2	7	_aCiencias biomédicas _0LocalX _2embne _9143729
650		7	_aMedicina _0LocalX _2embne _9405021
700	1		_aHrycay, Eugene G. _eeditor literario _0Local _993755
700	1		_aBandiera, Stelvio M. _eeditor literario _0Local _993756
830		0	_aAdvances in Experimental Medicine and Biology _x0065-2598 _v851 _9133153
856	4	0	_uhttps://go.openathens.net/redirector/universidadeuropea.es?url=https://link.springer.com/book/10.1007/978-3-319-16009-2 _zAcceso a este recurso digital (usuarios Universidad Europea de Madrid)
907			_a.b12899707 _b10-10-17 _c18-01-16
998			_am _a_alco _a_vill _b - - _cm _dz _e- _feng _ggw _h0
945			_aQP671.C83 M666 2015 EB _g1 _ieBOOK _j0 _lmae _o- _pEUR0.00 _q- _r- _sb _t15 _u0 _v0 _w0 _x0 _y.i11569323 _z06-04-17
999			_c81380 _d81380 _x1