Article View: sci.chem
Article #2253Re: equilibrium const for disulfide bond formation
From: hanson
Date: Fri, 12 Jan 2007 03:43
Date: Fri, 12 Jan 2007 03:43
60 lines
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3569 bytes
"Bob" <bbx107.XYZ@excite.XYZ.com> wrote in message news:5srdq2haa7beq0d40s2o9ipn1eobfki0br@4ax.com... > "hanson" <hanson@quick.net> wrote: > >>"Bob" <bbx107.XYZ@excite.XYZ.com> wrote in message >>news:a49bq2lve6k3skf7thuqronoo2csh4hq3a@4ax.com... >>> >>[Bob] >>> If you have it at fairly high concentration in an oxidizing >>> environment (air), and the Cys are exposed, one would expect that. >>> Solutions include keeping the conc low, avoiding oxidation -- and >>> reducing the dimers back to monomers, say with mercaptoethanol. >>> >>[hanson] >>Interesting. Are you basically telling here that the oxidized/dimer of >>Cysteine, now Cystine: HOOC(NH2)C-CH2-S-S-CH2-C(NH2)COOH >>together with 2 HS-CH2-CH2-OH disproportionates/redoxes into >> 2 HS-CH2-C(NH2)COOH and HO-CH2-CH2-S-S-CH2-CH2-OH. >> [Bob] > or heterodimers > > Note that the OP is talking about Cys in proteins, not free cystine. > The oxidation is dimerizing his protein (60 subunits to 120, in his > case). In other cases, it can create unwanted crosslinks within a > peptide chain. Major structural effects. > [hanson] >>Does HSEtOH work as a reducer for all -S-S- molecules in biologial >>systems? >> [Bob] > Yes, sort of. > > But a key point is that enzymes are large and BME > (beta-mercaptoethanol) is small. So one can easily have a vast molar > excess of BME. (You may recall that, typically, in enzyme reactions > the conc of substrate is a few order of magnitude higher than the > enzyme conc. Same idea.) Using it with small molecules, at similar > conc, would be more problematic. > > Bill Penrose has usefully elaborated. BME is simply one commonly > reducing agent. > > (But BME is doubly effective as a reducing agent. Not only does it > reduce disulfide bonds in the proteins, but it reduces the > concentration of people around you, thus making it easier for you to > concentrate on your work. The second effect is sometimes > irreversible.) > bob > [hanson] Bob, you are a good man. Thanks. I remember the smell faintly (though not being as bad a Et-SH), so, since I have left the lab long time ago, when I come back home from my stints in the field (deserts, mtns. or jungles, after a few weeks and 18 hrs flights), BME smells like roses when compared to me... ahaha... Thanks for the laughs, Bob, ahahaha... ahahanson
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X-Google-Thread: f4886,d004336369bd29fc X-Google-Thread: fd9c4,d004336369bd29fc X-Google-Attributes: gidf4886,gidfd9c4,public X-Google-Language: ENGLISH,ASCII-7-bit Path: arc1-ca.pugleaf.net!g2news2.google.com!news3.google.com!border1.nntp.dca.giganews.com!border2.nntp.dca.giganews.com!nntp.giganews.com!cyclone1.gnilink.net!spamkiller.gnilink.net!gnilink.net!trnddc07.POSTED!c101a669!not-for-mail From: "hanson" <hanson@quick.net> Newsgroups: sci.chem,bionet.molbio.proteins References: <1168370284.242721.50740@o58g2000hsb.googlegroups.com> <a49bq2lve6k3skf7thuqronoo2csh4hq3a@4ax.com> <T_iph.18043$Pe7.4055@trnddc04> <5srdq2haa7beq0d40s2o9ipn1eobfki0br@4ax.com> Subject: Re: equilibrium const for disulfide bond formation Lines: 62 X-Priority: 3 X-MSMail-Priority: Normal X-Newsreader: Microsoft Outlook Express 6.00.2900.3028 X-RFC2646: Format=Flowed; Original X-MimeOLE: Produced By Microsoft MimeOLE V6.00.2900.3028 Message-ID: <9tDph.16051$AM4.12522@trnddc07> Date: Fri, 12 Jan 2007 03:43:01 GMT NNTP-Posting-Host: 71.107.159.176 X-Complaints-To: abuse@verizon.net X-Trace: trnddc07 1168573381 71.107.159.176 (Thu, 11 Jan 2007 22:43:01 EST) NNTP-Posting-Date: Thu, 11 Jan 2007 22:43:01 EST