NONO键异裂能、均裂能的研究及硫亚硝基化合物（RSNO）对含巯基酶抑制作用的研究.pdf

用维生素C及含荧光基团的RSNO作为探针分子对RSNO与papain的作用进 行了深入的研究·令果证实这种抑制作用是由于酶的活性琉基基团直接进攻 RSNO中的硫原子，从而生成分子间的二硫键，使酶失活。这少果表明，RSNO 不光可以经过释放或转移 NO的途径 而且可以通过形成二硫键的途径来影响 蛋白质的结构与功能， 关键词: 键能，N-亚硝基脉 E-FAI叁R :一S-} , 酶，抑制 一 尹产别 StudyofN-NO,O-NOBondCleavageEnergiesandInhibitionof CysteineContainingEnzymesby5-Nitrosothiols By:MingMan Supervisor Prof Cheng,NankaiUniversity Prof.PengG.Wang,WayneStateUniversity NOistheonlymessengermoleculethatdoesnotdependonitsthree-dimensional structureintherecognitionandbindingprocess.NOcouldnotexistinalargequantityin humanbodyrfeely.Thismoleculehastobindtoacarriermoleculefirst,andthen,undera suitableenvironmentisreleasedtoanearbyreceptormoleculetocompletea transnitrosationcycle.Thus,itisessentialtoassessthebondingnatureofNOwithcarrier molecules,thebindingaffinities,themechanismofNOcapturebyNO-receptorsandNO- releasingrfomNO-donors,theratesforNOtransfer,andsoon.SinceNOisoneofthe simplestdiatomicmolecules,whenincontactwithanactivesiteinlivingsystems,it shouldnotbestronglyaffectedbystericorshape-dependentrecognitionfactorsthatlarge moleculesoftenencounter.ThismeansthatthedrivingforceforNOtransferrfomone moleculetoanotherwouldlargelydependonitsabilitytobindtotheparticularatomina molecule,whichisinvolvedintheNOtransportation. Inthisstudy,N-NObondcleavageenergiesofN-nitrosoureasandO-NObond cleavageenergiesofnitrosylcarboxylateshavebeenestimatedbydirectcalorimetric measurementscombinedwithrelevantelectrochemicaldata.Experimentalresultsindicate thattheN-nitrosoureacompoundshaveAH.sof52.4-62.0kcaVmol.TheOH,,correlates linearlywithpK,oftheparentcompound.N-NOhomolysisenergiesofallthemodel compoundsstudiedhere(25.4-33.1kcaUmol)aresubstantiallylowerthanthe correspondingheterolyticenergies,whichimpliesthatthebondhomolyticcleavagemust bemucheasiertotakeplacefortheseN-NOcompounds.Inthestudyofnitrosyl carboxylates,wefoundth