Abstract
The sulfhydryl group of the amino acid cysteine plays a pivotal role in the structure and function of numerous proteins. The high nucleophilicity of the thiolate anion coupled with its reasonably low pKa produces high chemical reactivity in nucleophilic additions and substitutions, accounting for its wide-spread use as a catalytic group in a variety of enzymes catalyzing hydrolysis, substitution, and exchange reactions. In addition, the reversible two electron oxidation converting the thiol of cysteine to its disulfide form is used not only in electron transfer reactions but also in crosslinking and stabilizing the tertiary and quarternary structure of proteins, the regulation of enzyme activity, and the protection of the intracellular environment. The direct application of electrochemical methods to the study of the redox properties of thiols, either in small molecules or in proteins, is complicated by interactions of the thiol with most electrode surfaces. Consequently, there have been few reliable electrochemical measurements of the redox potentials of cysteine and other biological thiols and disulfides. Nevertheless, alternate methodology involving reversible thiol/disulfide exchange equilibria has allowed the estimation of standard redox potentials of the sulfhydryl groups of biologically important thiols, including those found in proteins. In this chapter, the redox chemistry and biochemistry of the sulfhydryl groups of proteins will be outlined, methodology for applying the thiol/disulfide exchange reaction to the measurement of redox potentials will be described, and examples of the biological function of these redox state changes will be given.
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References
PC Jocelyn, Biochemistry of the Sulfhydryl Group, Academic Press, New York, 1972.
Yu M Torchinskii, Sulfhydryl and Disulfide Groups of Proteins, Plenum, New York, 1974.
H Sies, Angew. Chem. Int. Ed. Engl. 25 (1986) 1058–1064.
A Meister and ME Anderson, Annu. Rev. Biochem. 52 (1983) 711–760.
B Chance, H Sies and A Boveris, Pysiol. Rev. 59 (1979) 527–605.
CH Williams in The Enzymes, PD Boyer (ed), Academic Press, New York, 1976, Vol 13, pp. 89–174.
L Eldjan and A Phil, J. Amer. Chem. Soc. 79 (1957) 4589–4593.
ES Guzman Barron, Adv. Enzymol. 11 (1951) 201–266.
M Freidman, The Chemistry and Biochemistry of the SH Group, Pergamon Press, Elmsford, New York, 1973.
HF Gilbert, Adv. Enzymol. 63 (1990) 69–172.
NS Kosower and EM Kosower, Int. Rev. Cytol. 54 (1978) 109–160.
DM Ziegler, Annu. Rev. Biochem. 54 (1985) 305–329.
BB Buchanan, Ann. Rev. Plant Physiol. 31 (1980) 341–374.
HF Gilbert, Methods Enzymol. 107 (1984) 330–351.
H Eggerer and A Klette, Eur. J. Biochem. 1 (1967) 447–453.
A Klug and D Rhodes, Trend. Biol. Sci. 12 (1987) 464–469.
RC Fahey in Protein Crosslinking: Biochemical and Molecular Aspects, part A, Plenum Publishing Corp., New York, 1977, pp. 1–30.
DJ Reed and PW Beatty in Reviews in Biochemical Toxicology, E Hodgson, JR Bend, and RM Philpot (eds), Elsevier, New York, 1980, pp. 231–242.
JM Thornton, J. Mol. Biol. 151 (1981)261–287.
DB Volkin and AM Klibanov, J. Biol. Chem. 262 (1987) 2945–2950.
CN Pace, Sci. 15 (1990) 14–17.
CB Anfinsen and HA Scheraga, Adv. Protein Chem. 29 (1975) 205–225.
TE Creighton, Prog. Biophys. Mol. Biol. 33 (1978) 231–297.
CA Marks, H Naderi, PA Kosen, ID Kuntz and S Anderson. Science 235 (1987) 1370–1373.
FG Hopkins and M Dixon, J. Biol. Chem. 54 (1922) 527–563.
LE Anderson in Thioredoxin and Glutaredoxin Systems: Structure and Function, A Holmgren (ed), Raven Press, New York, 1986, pp 26–37.
H Sies, R Brigelius and P Graf, Adv. Enzyme Reg. 26 (1987) 175–189.
HF Gilbert, J. Biol. Chem. 257 (1982) 12086–12091.
DW Walters and HF Gilbert, J. Biol. Chem. 261 (1986) 12135–13143.
RE Cappel and HF Gilbert, J. Biol. Chem. 265 (1990) 15464–15470.
F Daniels and RA Alberty, Physical Chemistry, 3rd Edition, John Wiley and Sons, New York, 1966, p. 241.
J Houk and GM Whitesides, J. Amer. Chem. Soc. 109 (1987) 6825–6836.
GH Snyder, Biochemistry 26 (1987) 688–694.
WW Cleland, Biochemistry 3 (1964) 480–483.
DM Rothwarf and HA Scheraga, Proc. Natl. Acad. Sci. USA 89 (1992) 7944–7948.
MH Chau and JW Nelson, FEBS Lett. 291 (1991) 296–298.
EM Scott, IW Duncan and V Ekstrand, J. Biol. Chem. 238 (1963) 3928–3933.
G Gorin, A Esfandi and GB Guthrie, Arch. Biochem. Biophys. 168 (1975) 450–454.
WM Clark, Oxidation-Reduction Potentials of Organic Systems, The Williams and Wilkins Co., Baltimore, 1960, p. 486.
IM Kolthoff and C Barnum, J. Amer. Chem. Soc. 62 (1940) 3061–3066.
GT Rogers and DN Mallett, Bioelectrochem. Bioenerg. 10 (1983) 269–277.
RP Szajewski and GM Whitesides. J. Amer. Chem. Soc. 102 (1980) 2011–2026.
HA Scheraga, Y Konishi and T Ooi, Adv. Biophys. 18 (1984) 21–41.
TE Creighton, Meth. Enzymol. 107 (1984) 305–329.
JS Weissmann and PS Kim, Science 253 (1991) 1386–1393.
JA Wells and DB Powers, J. Biol. Chem. 261 (1986) 6564–6570.
DW Walters and HF Gilbert, J. Biol. Chem. 261 (1986) 15372–15377.
MW Collison, D Beidler, LM Grimm and JA Thomas, Biochim. Biophys. Acta 885 (1986)58–67.
DJ Hupe and ER Pohl, Isr. J. Chem. 26 (1986) 395–399.
RE Cappel and HF Gilbert, J. Biol. Chem. 261 (1986) 15378–15384.
PC Jocelyn, Eur. J. Biochem. 2 (1967) 327–333.
IM Kolthoff, W Stricks and RC Kapoor, J. Amer. Chem. Soc. 77 (1955) 4733–4741.
L Eldjarn and A Phil, J. Amer. Chem. Soc. 79 (1957) 4589–4595.
P Eyer and D Podhradsky, Anal. Biochem. 153 (1986) 57–61.
R Zhang and GH Snyder, Biochemistry 27 (1988) 3785 - 3794.
Y Goto and K Hamaguchi, J. Mol. Biol. 146(1981)321–327.
ME O’Donnell and CH Williams, J. Biol. Chem. 258 (1983) 13795–13805.
RG Matthews and CH Williams, J. Biol. Chem. 251 (1976) 3956–3964.
SM Miller, DP Ballou, V Massey, CH Williams and CT Walsh, J. Biol. Chem. 261 (1986) 8081–8084.
A Holmgren, J. Biol. Chem. 254 (1979) 3672–3678.
A Holmgren, Meth. Enzymol. 107 (1984) 295–300.
HE Huber, M Russel, P Model and CC Richardson, J. Biol. Chem. 261 (1986) 15006–15012.
F Rebeille and MD Hatch, Arch. Biochem. Biophys. 249 (1986) 164–170.
CJ Clancey and HF Gilbert, J. Biol. Chem. 262 (1987) 13545–13551.
AH Fairlamb, P Blackburn, P Ulrich, BT Chait and A Cerami, Science 227 (1985) 1485–1487.
TE Creighton, Functions of Glutathione: Biochemical, Physiological, Toxicological, and Chemical Aspects, A Larsson, S Orrenius, A Holmgren and B Mannervik (eds), Raven Press, New York, 1983, pp. 205–213.
CN Pace and TE Creighton, J. Mol. Biol. 188 (1986) 477–486.
RT Sauer, K Hehir, RS Stearman, MA Weiss, A Jeitler-Nilsson, EG Suchandek et al., Biochemistry 25 (1986) 5992–5998.
RE Cappel, JW Bremer. TM Timmons, TE Nelson and HF Gilbert, J. Biol. Chem. 261 (1986) 15385–15389.
RE Cappel and HF Gilbert, J. Biol. Chem. 264 (1989) 9180–9187.
RE Cappel and HF Gilbert, J. Biol. Chem. 263 (1988) 12204–12212.
MM Lyles and HF Gilbert, Biochemistry 30 (1991) 613–619.
A Zapun, JCA Bardwell and TE Creighton, Biochemistry 32 (1993) 5083–5092.
MI Page and WP Jencks, Biochem. Biophys. Res. Commun. 57 (1974) 887–889.
TE Creighton, Meth. Enzymol. 131 (1986) 83–104.
PJ Milburn, YC Meinwald, S Takahashi, T Ooi and HA Scheraga, Int. J. Peptide Protein Res. 31 (1988) 311–321.
DC Poland and HA Scheraga, Biopolymers 3 (1965) 379–399.
PN Kao and A Karlin, J. Biol. Chem. 261 (1986) 8085–8088.
JM Wilson, RJ Bayer and DJ Hupe, J. Amer. Chem. Soc. 99 (1977) 7922–7926.
HF Gilbert, Biochemistry 28 (1989) 7298–7305.
WP Jencks, Proc. Natl. Acad. Sci. USA 78 (1981) 4046–4050.
BA Katz and A Kossiakoff, J. Biol. Chem. 261 (1986) 15480–15485.
PJ Milburn, Y Konishi, YC Meinwald and HA Scheraga, J. Amer. Chem. Soc. 109 (1987) 4486–4496.
A Holmgren in Thioredoxin and Glutaredoxi Systems: Structure and Function, A Holmgren (ed), Raven Press, New York, 1986, pp. 1–9.
A Holmgren and M Fagerstedt, J. Biol. Chem. 257 (1982) 6926–6933.
EA Newsholm and C Start, Regulation in Metabolism, John Wiley, London, 1973, p. 325.
I Carlberg and B Mannervik, Meth. Enzymol. 113 (1985) 484–489.
RA Karplus and GE Schulz, J. Mol. Biol. 195 (1987) 701–729.
AJ Alpert and HF Gilbert, Anal. Biochem. 144 (1985) 553–562.
N Nitateishi, T Higashi, S Shinya, A Naruse and Y Sakamoto, J. Biochem. (Tokyo) 75 (1974) 93–103.
RJ Jaeger, RB Connolly and SD Murphy, Res. Commun. Chem. Pathol. Pharmacol. 6 (1973)465–467.
H Sies, Oxidative Stress, Academic Press, London, 1985.
V Massey and CH Williams, J. Biol. Chem. 240 (1965) 4470–4480.
B Mannervik, Acta Chem. Scand. 23 (1969) 2912–2914.
PM Chung, RE Cappel and HF Gilbert, Arch. Biochem. Biophys. 288 (1991) 48–53.
PG Penketh, WPK Kennedy, CL Patton and AC Sartorelli, FEBS Lett. 221 (1987) 427 - 432.
SL Shames, AH Fairlamb, A Cerami and CT Wash, Biochemistry 25 (1986) 3519–3526.
M Droux, M Miginiac-Maslow, JP Jacquot, P Gadal, NA Crawford, NS Kosower et al., Arch. Biochem. Biophys. 256 (1987) 372–380.
L Thelander and P Reichard, Ann. Rev. Biochem. 48 (1979) 133–202.
J Stubbe, Adv. Enzymol. 63 (1990) 349–419.
L Thelander, J. Biol. Chem. 249 (1974) 4858–4862.
AN Lin, GW Ashley and J Stubbe, Biochemistry 26 (1987) 6905–6909.
A Holmgren, BO Soderberg, H Klund and CI Branden, Proc. Natl. Acad. Sci. USA 72 (1990) 2305–2309.
HJ Dyson, GP Gippert, DA Case, A Holmgren and PE Wright, Biochemistry 29 (1990) 4129–4135.
RF Kelley, W Shalongo, MV Jagannadham and E Stellwagen, Biochemistry 26 (1887) 1406–1411.
G Krause, J Lundstron, JL Barea, CP de la Cuesta and A Holmgren, J. Biol. Chem. 266 (1991) 9494–9500.
O Berglund and A Holmgren, J. Biol. Chem. 250 (1975) 2778–2782.
S Tabor, HE Huber and CC Richardson, J. Biol. Chem. 262 (1987) 16212–16223.
K Maeda, A Tsugita, A Dalzoppo, F Vilbois and P Schurmann, Eur. J. Biochem. 154 (1986) 197–203.
J Buc, M Riviere, B Gontero, P Sauve, J-C Meunier and J Ricard, Eur. J. Biochem. 140 (1984) 199–202.
A Holmgren, J. Biol. Chem. 254 (1979) 3664–3670.
B Kren, D Parsell and JA Fuchs, J. Bacteriol. 170 (1988) 308–315.
JO Hishoishog, H von Bahr-Lindstrishom, H Jhornvall and A Holmgren, Gene 43 (1986) 13–21.
H Tabor, J. Biol. Chem. 250 (1975) 2648–2658.
AH Fairlamb, GB Henderson and A Cerami, Mol. Biochem. Parasitol. 21 (1986) 247–257.
AH Fairlamb and GB Henderson in Host-Parasite Cellular and Molecular Interactions in Protozoal Infections, KP Chang and D Snary (eds), Springer-Verlag, New York, 1987, pp. 29–40.
CB Anfinsen, E Haber, M Sela and FH White, Proc. Natl. Acad. Sci. USA 47 (1961) 1309–1314.
TE Greighton, Proteins, Structures and Molecular Properties, WH Freeman, New York, 1984, Chap. 7.
VP Saxena and DB Wetlaufer, Biochemistry 9 (1970) 5015–5023.
Y Konishi, T Ooi and HA Scheraga, Biochemistry 21 (1982) 4734–4780.
DB Wetlaufer, PA Branca and G-X Chen, Protein Engineering 1 (1987) 141–146.
TE Creighton, J. Mol. Biol. 113 (1977)329–341.
HF Gilbert in Mechanisms of Protein Folding, RH Pain (ed) Oxford: RL Press (1994) pp. 104–136.
TY Lin and PS Kim, Biochemistry 28 (1989) 5282–5287.
R Wetzel, Trend. Biol. Sci. 12 (1987) 478–482.
CO Pabo and EG Suchanek, Biochemistry 25 (1987) 5987 - 5991.
JE Villafranca, EE Howell, DHY Voet, MS Strobel, RC Ogden, JN Abelson et al., Science 222 (1983) 782–788.
R Wetzel, LJ Perry, WA Baase and WJ Becktel, Proc. Natl. Acad. Sci. USA 85 (1988) 401–405.
M Matsumura, WJ Becktel, M Levitt and BW Matthews, Proc. Natl. Acad. Sci. USA 86 (1989) 6562–6566.
M Matsumura, G Signor and BW Matthews, Nature 342 (1989) 291–293.
GE Edwards, H Nakamoto, JN Burnell and MD Hatch, Annu. Rev. Plant Physiol. 36 (1985) 255–286.
R Scheibe, FEBS Lett. 133 (1981) 301–304.
R Rebeille and MD Hatch, Arch. Biochem. Biophys. 249 (1986) 171–179.
BB Buchanan, P Schurmann and PP Kalberer, J. Biol. Chem. 246 (1971) 5952–5959.
C Foyer and B Halliwell, Planta 133 (1976) 21–25.
B Halliwell and CH Foyer, Planta 139 (1978) 9–17.
CJ Batie and H Kamin, J. Biol. Chem. 261 (1986) 11214–11223.
RA Wolosiuk, NA Crawford, BC Yee and BB Buchanan, J. Biol. Chem. 254 (1979) 1627–1632.
D Di Monte, G Bellomo, H Thor, P Nicotera and S Orrenius, Arach. Biochem. Biophys. 235 (1984) 343–350.
NS Kosower, GA Vanderhoff and EM Kosower, Biochim. Biophys. Acta 272 (1972) 623–630.
GL Francis and FJ Ballard, Biochem. J. 186 (1980) 581–586.
H Sies and KH Summer, Eur. J. Biochem. 57 (1975) 503–512.
R Brigelius, Hoppe Seyler’s. Z. Physiol. Chem. 364 (1983) 989–996.
M Usami, H Matsushita andT Shimazu, J. Biol. Chem. 255 (1980) 1928–1934.
C Abate, L Patel, FJ Rauscher and T Curran, Science 249 (1990) 1157–1161.
KA Hutchison, G Matic, S Meshinchi, EH Bresnick and WB Pratt, J. Biol. Chem. 266 (1991)10505–10509.
TH Rushmore, MR Morton and CB Pickett, J. Biol. Chem. 266 (1991) 11632–11639.
ME Anderson, Meth. Enzymol. 113 (1985) 548–554.
TPM Akerboom, M Bilzer and H Sies, J. Biol. Chem. 257 (1982) 4248–4252.
BH Lauterburg, JD Adams and JR Mitchell, Hepatology 4 (1984) 586–590.
R Brigelius in Oxidative Stress, Academic Press, London, 1985, pp. 243–270.
DJ Reed and MW Fariss, Pharmacol. Rev. 36 (1984) 25S–32S.
JL Plummer, BR Smith, H Sies and JR Bend, Meth. Enzymol. 77 (1981) 50–59
A Meister, Meth. Enzymol. 113 (1985) 571–580.
OW Griffith, RJ Bridges and A Meister, Proc. Natl. Acad. Sci. USA 76 (1979) 6319–6322.
P Apontoweil and W Berends, Biochim. Biophys. Acta 399 (1975) 10.
S Orrenius, AA Jewell, H Thor, G Bellomo, L Eklow and MT Smith in Isolation, Characterization, and Use of Hepatocvtes, RA Harris and NW Cornell (eds), Elsevier, New York, 1983, pp 333–340.
R Brigelius, C Muckel, TPM Akerboom and H Sies, Biochem. Pharm. 32 (1983) 2529–2534.
MJ Meredith, Anal. Biochem. 131 (1983) 504–509.
T Higashi, M Furukawa, A Hikita, N Naruse, N Tateishi and Y Sakamoto, J. B iochem. (Tokyo) 257 (1983) 1661–1667.
MF Lou, LL Poulsen and DM Ziegler, Meth Enzymol. 143 (1987) 124–129.
E-M Park and JA Thomas, Biochim. Biophys. Acta 964 (1988) 151–160.
K Rokutan, JA Thomas and H Sies, Eur. J. Biochem. 179 (1989) 233–239.
YC Chai, CH Jung, CK Lii, SS Ashraf, S Hendrich, B Wolf et al. Arch. Biochem. Biophys. 284 (1991) 270–278.
RG Kemp, Meth. Enzymol. 42 (1972) 71–80.
HF Gilbert and MD Stewart, J. Biol. Chem. 256 (1981) 1782–1785.
CF Tormanen andTJ Scallen, Circulation 64 (1980) VI271.
I Dotan and I Shechter, Arch. Biochem. Biophys. 226 (1983) 401–410.
J Roitelman and I Shechter, J. Biol. Chem. 259 (1984) 870–877.
GC Ness, SJ Eales, LC Pendleton and M Smith, J. Biol. Chem. 260 (1985) 12391–12393.
I Dotan and 1 Schechter, J. Biol. Chem. 262 (1987) 17058–17064.
TJC Van Berkel, JF KosterandGEJ Staal, Biochim. Biophys. Acta 321 (1973)496–501.
JS Bond, J. Biol. Chem. 259 (1984) 886–891.
S Pontremoli, E Melloni, M Michetti, F Salamino, B Sparatore and BL Horecker, Arch. Biochem. Biophys. 213 (1982) 731–733.
Y Ozaki, A Mizuno, K Itoh and K Iriyama, J. Biol. Chem. 262 (1987) 15445–15551.
K Axelsson, S Eriksson and B Mannervik, Biochemistry 17, 2978, 1978.
ZR Gan and WW Wells, J. Biol. Chem. 261 (1986) 996–1001.
ZR Gan and WW Wells, J. Biol. Chem. 263 (1988) 9050–9054.
Y Yang and WW Wells, J. Biol. Chem. 265 (1990) 589–593.
M Luthman and A Holmgren, J. Biol. Chem. 257 (1982) 6686–6690.
ZR Gan and WW Wells, J. Biol. Chem. 262 (1987) 6699–6703.
YF Yang and WW Wells, J. Biol. Chem. 266 (1991) 12766–12772.
JJ Mieyal, DW Starke, SA Gravina, C Dothey and JS Chung, Biochemistry 30 (1991) 6088–6097.
DA Hillson, N Lambert and RB Freedman, Meth. Enzymol. 107 (1984) 281–300.
JE Morin and JE Dixon, Meth. Enzymol. 113 (1985) 541–547.
PT Varandani in Mechanisms of Oxidizing Enzymes, TP Singer and RN Ondarza (eds), Elsevier, Amsterdam, 1978, pp. 29–35.
RB Freedman and DA Hillson in The Enzymology of Post-translational Modification of Proteins, RB Freedman and HC Hawkins (eds), Academic Press, New York, 1980, Vol I, pp. 157–212.
S Bjelland, K Wallevik, J Kroll, JE Dixon, JE Morin, RB Freedman et al., Biochim. Biophys. Acta 747 (1983) 197–199.
RB Freedman, Trend Bioch. Sci. 9 (1984) 438–441.
JC Edman, L Ellis, RW Blacher, RA Roth and WJ Rutter, Nature 317 (1985) 267–270.
JI Morris and PT Varandani, Biochim. Biophys. Acta 949 (1988) 169–180.
R Roth and S Pierce, Biochemistry 26 (1987) 4179–4182.
J Koivu and R Mullyla, J. Biol. Chem. 262 (1987) 6159–6164.
JR Wetterau, KA Combs, SN Spinner and BJ Joiner, J. Biol. Chem. 265 (1990) 9800–9807.
T Obata, S Kitagawa, QH Gong and I Pastan, J. Biol. Chem. 263 (1988) 782–785.
M Geeth-Habib, R Novia, HA Kaplan and WJ Lennarz, Cell 54 (1988) 1053–1060.
TE Creighton, DA Hillson and RB Freedman, J. Mol. Biol. 142 (1990) 43–48.
HC Hawkins, M deNardi and RB Freedman, Biochem. J. 275 (1991) 1991–1998.
JC Bardwell, K McGovern and J Beckwith, Cell 67 (1991) 581–589.
DM Ziegler and LL Poulson, Trend Biol. Sci. 2 (1977) 79–81.
WW Wells, DP Xu, Y Yang and PA Rocque, J. Biol. Chem. 265 (1990) 153–157.
VP Pigiet and BJ Schuster, Proc. Natl. Acad. Sci. USA 83 (1986) 7643–7647.
HC Hawkins, EC Blackburn and RB Freedman, Biochem J. 275 (1991) 349–353.
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Gilbert, H.F. (1997). Thiol/disulfide exchange and redox potentials of proteins. In: Lenaz, G., Milazzo, G. (eds) Bioelectrochemistry of Biomacromolecules. Bioelectrochemistry: Principles and Practice, vol 5. Birkhäuser Basel. https://doi.org/10.1007/978-3-0348-9179-0_5
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