Physical Chemistry Introduction to Quantum Mechanics
Physical Chemistry Introduction to Quantum Mechanics CHEM 113A
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This 27 page Class Notes was uploaded by Michael Reilly on Friday September 4, 2015. The Class Notes belongs to CHEM 113A at University of California - Los Angeles taught by Staff in Fall. Since its upload, it has received 124 views. For similar materials see /class/177989/chem-113a-university-of-california-los-angeles in Chemistry at University of California - Los Angeles.
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Date Created: 09/04/15
hemoglobin and myoglobin vertebrates and other fix NJ Hemocyanin molluscs and aIthropods Hemerythrin sea worms gFem M NH HNWN 39 V N HN 24m o 07 N7 1 NH 1 X1 1 Y m 16H 2 PC 7 FN AA A v n T Th heme group 111 sperm mm myoglobin u The hams b hon prowporphynn 1X group is the active site ofmyuglobm 17 The 1mm h gluup m m a cleft fanned by halxces E and F gt m m1 chains the pmxml His H 3 and me disml His H64 are s mwn Xnr Mb m1 H15 and sits inside the Inland 0 uxy n We molecule 1 lydrugsn bon ed 0 ll 1 bmding mg pocket 1 pocket The wew m dileclly mm the lxgzmdbind u Closeup ofthe active sue Dr dcoxyMb PDB conic IAGN In nddluon to me distal Hm l Lcu L20 vlll VGSL ml a P11 13945 1m 11 llgdndblndlng pockcl d Clam ohh am m ofoxyM l l T c cuurdlmlc d l lvdmgen bands to l s lsLal HIS Note how m p in ing 01 0 39 v a 396 w re ll hulidn es m often desmmled by max pasi ion un he hellx a manner Illa is mdependem m the specles 01 Mb m H m dlslul Hls Is the sevemh mulls along helm I and ls dcnmed lawns analogousl 1hr proxmml H s ls denoled EXHls Routes to irreversible oxidation of Fell porphyrins Bimolccular contact of two F c porphyn39n moieties PFCO l PFC Pch o chP Nuclcophilic displacement both by SN and SXZ mechanisms PFcOg l X PchX I 03quot Electron transfer PFC Pch l c a a mm H W Um Mm my m m n V m Im 1 My MMHMI39uvnmvmh v mm ywwwmlWqu wwwm Mm anrmrmw 0mmmvm hw17 W m mum wl m HquotI II I1ML V umvmmw Mm hcmuumhd Lama Uu mm mm m lhrw nrmunut u w rm mmm k we 3 Mg hmmuu mm um m m um m mu y mm m m m M 1Hmm uw a m mw hemoglobin and myoglobin vertebrates and other fix NJ Hemocyanin molluscs and aIthropods Hemerythrin sea worms gFem M NH HNWN 39 V N HN 24m o 07 N7 1 NH 1 Flg XMj myqummmm M m a m b c w n w urr HIKmm Oxyhemerylhrin of the sipun ctllid worm Themixtc OWEN IPDB code lHMO oxy IHMD deoxy a One sub unit of the outameric protein 7 Closeup of the active site showing the manner by which 03 is bound to a single Fe atom and is hydrogen bonded to the bridging 0x0 moiety O rum m Fe mm D H1573 As 139 D u 0 sum Deuxyhemerymrin Ems Oxyhemerylh rm Examples of Dioxygen Activating Monooxygenase Enzymes 02 gt 2H 26 0 H20 C0039 0 NH NHa NHa 02 gt 4 2H 2e OH 0 OH H20 OH 0 O 2H 2e 0H OH H20 Catalyzed by Cytochrome P450 Tyrosinase Methane monooxygenase W 7 lth Dnuxy emucynnln am rcdunnd 39yms nnsn Iv unosecy Fiducd MMC H mm mu x51 AdvL 5m mm m Lnuwn o m cummwm In Mr H mm un 1 H mm mm mmqu n 1 m m r 0H mum Kinetics of dioxygen reactions oDirect reactions of dioxygen tend to be slow because ground state dioxygen is a triplet and most reactants are singlets 302ll 1X H 1XO2H triplet singlet It is impossible for this spin forbidden reaction to go in one concerted step Proposed Mechanisms heme diiron dicopper II II reduced Fe o O39Fe VCU39 Cutw enzyme r 021 02 metaquot FemO Q FeIll quot0 ll peroxo o 0 Cu Cu species Y high valent lvOx IV urox lll metaloxo Fe O IFe cu 0 cu intermediate Y Figure 1 Unified mechanistic scheme for dioxygen activation at metaiioenzyme active sites r 0 mm mm hgm 39andv hguml 10 an 1 UN 41 E xgln mg m mm d Nolelhal a g 1 Wm LId 151ml predxm 1x 1iv 1 whielhc anp e hgfmd 1mm mwriu mm mm wmnamzms smngw Jay 12th s a powerful fourelectron 0 ng agent 4e4Ho2 a 2H20 AG39 kcalmol oz u 1 z a 4 Number of electrons added Cytochrome P450 Fig X53 Catalytic mechanism f 0139 Cytochrome P450 2 4 H2 2H 23 H O O H H R H High spin gt Fem e Few SCys SCVS 2 r R H P450m 0H2 H20 2 R H J peroxide nl Low spln gt Fequot shunt 1 Fen 1 80515 i SCys P e l 2H 39 P 450ox HH oxy 450 ll Rh FBN H2 H2 SCys Pomon of the crystst structure d PASOW wtb bound substrate showmg the heme and brotern cysterne rgstrorr of tron Newcomb M Toy PH W 2000 33 44955 Hypersenstwe rsdrcst probes and the mechamsms of cytochrome P450cststyzeo bydroxytstrorr resotrons w k mleraclions unpumml for he helemlysls of the 070 bond quotOH v m Fea L H H20 27 27 2 0 C Cr L def or or 1 ij L L L mm P eu gew cm m m52g zam0 Fig 1051 Nam hm We rmyw nxygen Kpunml m y MM Iway mun lhe s umydmgsr v 39dr n plm Oxygen rebound mechanism Cys 05 abstraction rebound R I I I Hi Jana MEWS RNFi ERa Direct oxygen insertion Mic M 0 C M i Ci H O i H wcomb M Toy PH Acc Chem Res 2000 3344955 Hypersensitive radical probes and the mechanisms of cytochrome P450catalyzed hydroxylation reactions Q 1095quot Q gt 3X1010571 I gt E39 saxiow s1 M gt H020 ROQC i 1 4gtlt1O11s1 A gt Arm Ar V ca4x101251 O Some ultrafast radical rearrangements Rate constants shown above the arrows are for reactions at ambient temperature 0 Fequot Ile H W Cquot X X Fe H u oio H H O F N F w Fem X X X Cymchmme Heme peruxidases P450 cytochrome P450 Heme oxygenase aromatase Proposed active species that may form upon oneelectron reduction of oxyheme enzymes
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