Rapid Reaction Kinetics: Lessons Learnt from Ion Pumps
Ronald J. ClarkeSchool of Chemistry, University of Sydney, Sydney, NSW 2006, Australia. Email: r.clarke@chem.usyd.edu.au
Australian Journal of Chemistry 64(1) 5-8 https://doi.org/10.1071/CH10271
Submitted: 19 July 2010 Accepted: 21 October 2010 Published: 14 January 2011
Abstract
Chemical kinetics underwent a revolution in the 1950–60s with the development by Manfred Eigen of relaxation kinetic techniques and theory for the analysis of the results obtained. The techniques he introduced extended the time scale of measurable reactions into the microsecond range and beyond. Since then, computing power has increased astronomically. Some of the approximations traditionally used in the analysis of relaxation kinetic data to reduce mathematical complexity are, therefore, now no longer a necessity. Numerical integration of coupled series of differential rate equations can be performed in seconds or less on desk-top computers. In research on the mechanism of the Na+,K+-ATPase, it has been found that traditional approaches to relaxation kinetic data can sometimes lead to erroneous conclusions or to an incomplete description of the mechanism. Therefore, one needs to be flexible in one’s approach to kinetic data analysis and carefully consider the validity of any approximations used.
References
[1] Laidler K. J., Chemical Kinetics, 3rd edn 1987 (HarperCollins: New York, NY).[2] M. Eigen, Discuss. Faraday Soc. 1954, 17, 194.
| Crossref | GoogleScholarGoogle Scholar |
[3] M. Eigen, Q. Rev. Biophys. 1968, 1, 3.
| Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaF1cXkvVenur0%3D&md5=8ccaa1e3daa4ab65ff6bf17b9d535b7fCAS | 4885733PubMed |
[4] Bernasconi C. F., Relaxation Kinetics 1976 (Academic Press: New York, NY).
[5] Strehlow H., Rapid Reactions in Solution 1992 (VCH: Weinheim).
[6] L. Michaelis, M. L. Menten, Biochem. Z. 1913, 49, 333.
| 1:CAS:528:DyaC3sXhsFaqtw%3D%3D&md5=f9f82c4ceec455bb8c54c93eb8d6415cCAS |
[7] G. E. Briggs, J. B. S. Haldane, Biochem. J. 1925, 19, 338.
| 1:CAS:528:DyaB2MXhsFyjsw%3D%3D&md5=e4901be2baa15fc458ef4ca08074ca53CAS | 16743508PubMed |
[8] R. J. Clarke, D. J. Kane, Biophys. J. 2007, 93, 4187.
| Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD1cXhvVA%3D&md5=aef61e4f7ff0b701b25e8de148651308CAS | 17766357PubMed |
[9] A. Pilotelle-Bunner, J. M. Matthews, F. Cornelius, H.-J. Apell, P. Sebban, R. J. Clarke, Biochemistry 2008, 47, 13103.
| Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD1cXhtlGqsLrJ&md5=d658f69301c1a300b3ae5a2185881587CAS | 19006328PubMed |
[10] N. U. Fedosova, P. Champeil, M. Esmann, Biochemistry 2002, 41, 1267.
| Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD3MXpt1CnsLs%3D&md5=d1a738d4d77ae6e1b324b27f8c907a28CAS | 11802726PubMed |
[11] K. Fendler, S. Jaruschewski, A. Hobbs, W. Albers, J. P. Froehlich, J. Gen. Physiol. 1993, 102, 631.
| Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaK2cXjtFyisbc%3D&md5=15b6c91f430101fb6b36ea4ab738c007CAS | 8270908PubMed |
[12] T. Friedrich, E. Bamberg, G. Nagel, Biophys. J. 1996, 71, 2486.
| Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaK28XmslGgtr0%3D&md5=d206d0453e1dcf1a4af2a0ceda17077aCAS | 8913588PubMed |
[13] D. J. Kane, K. Fendler, E. Grell, E. Bamberg, K. Taniguchi, J. P. Froehlich, R. J. Clarke, Biochemistry 1997, 36, 13406.
| Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaK2sXmsVehur0%3D&md5=69068c872525217b488a436bd5404e3cCAS | 9341234PubMed |
[14] R. J. Clarke, D. J. Kane, H.-J. Apell, M. Roudna, E. Bamberg, Biophys. J. 1998, 75, 1340.
| Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaK1cXlvVCru78%3D&md5=e6055f01e642b4ecdb7dd63b16af989dCAS | 9726935PubMed |
[15] R. J. Clarke, H.-J. Apell, B. Y. Kong, Biochemistry 2007, 46, 7034.
| Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD2sXlsVKjtrc%3D&md5=0c59ebc9205227ab9fcd116733aa6575CAS | 17511477PubMed |
[16] M. Khalid, F. Cornelius, R. J. Clarke, Biophys. J. 2010, 98, 2290.
| Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BC3cXosFCitr4%3D&md5=f63be369dc5d6b00ff8d984aa5462024CAS | 20483338PubMed |
[17] C. Hegyvary, R. L. Post, J. Biol. Chem. 1971, 246, 5234.
| 1:CAS:528:DyaE3MXltlOis7c%3D&md5=ae63ff45594e634b27c11b1220586048CAS | 4255317PubMed |
[18] R. L. Post, C. Hegyvary, S. Kume, J. Biol. Chem. 1972, 247, 6530.
| 1:CAS:528:DyaE3sXhsVOj&md5=2f5811b469cf5ba117f2b91711e15a20CAS | 4263199PubMed |
[19] S. J. D. Karlish, D. W. Yates, I. M. Glynn, Nature 1976, 263, 251.
| Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaE2sXjvFehtw%3D%3D&md5=89831a25aaa9a09605e731e66c1d4eb6CAS | 134290PubMed |
[20] S. J. D. Karlish, D. W. Yates, I. M. Glynn, Biochim. Biophys. Acta 1978, 525, 252.
| 1:CAS:528:DyaE1cXltVakt7k%3D&md5=e8048bb64a84a2145a075c18927b1ab5CAS | 210812PubMed |
[21] S. J. D. Karlish, D. W. Yates, Biochim. Biophys. Acta 1978, 527, 115.
| 1:CAS:528:DyaE1MXjsFGlsw%3D%3D&md5=db49f39044b7b0926a98b4daf157f60fCAS | 214132PubMed |
[22] M. Steinberg, S. J. D. Karlish, J. Biol. Chem. 1989, 264, 2726.
| 1:CAS:528:DyaL1MXhvVynsbs%3D&md5=06b6f6e4b04ca285f69a92467fc0ae80CAS | 2536722PubMed |
[23] P. A. Humphrey, C. Lüpfert, H.-J. Apell, F. Cornelius, R. J. Clarke, Biochemistry 2002, 41, 9496.
| Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD38XkvFClsbY%3D&md5=a297b2d0fabfdfa193993d58cdab5bd0CAS | 12135372PubMed |
[24] R. M. González-Lebrero, S. B. Kaufman, M. R. Montes, J. G. Nørby, P. J. Garrahan, R. C. Rossi, J. Biol. Chem. 2002, 277, 5910.
| Crossref | GoogleScholarGoogle Scholar | 11739377PubMed |
[25] M. R. Montes, R. M. González-Lebrero, P. J. Garrahan, R. C. Rossi, Biochemistry 2004, 43, 2062.
| Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD2cXnsVGqtw%3D%3D&md5=eb222ce7d18eac1ee64e32fcffa53d27CAS | 14967046PubMed |
[26] R. J. Clarke, Eur. Biophys. J. 2009, 39, 3.
| Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD1MXhtlymurrP&md5=376b3049e89a55d35a182ea040a92e40CAS | 19225774PubMed |
