Increase in apparent compressibility of cytochrome c upon oxidation
- PMID: 6278497
- PMCID: PMC345843
- DOI: 10.1073/pnas.79.3.815
Increase in apparent compressibility of cytochrome c upon oxidation
Abstract
The apparent molal adiabatic compressibilities of ferri- and ferrocytochrome c have been determined from measurements of density and sound velocity. The values found were +2.99 X 10(-8) and -2.40 X 10(-8) cm5 mol-1 dyne-1 for the ferri and ferro forms, respectively. Experiments were performed on identical solutions containing either the oxidized or reduced form of protein. Solutions of ferricytochrome c were found to have significantly greater adiabatic compressibility than equivalent solutions of ferrocytochrome c at 25 degrees C and pH 7.15. The remarkable similarity of the three-dimensional structures of the ferri and ferro proteins [Takano, T. & Dickerson, R.E. (1980) Proc. Natl. Acad. Sci. USA 77, 6371-6375] strongly suggests that this difference in compressibility is due to an increase in volume fluctuations within ferricytochrome c relative to the ferro form rather than a change in equilibrium structure or hydration. Such a difference in the dynamic properties of the structures is consistent with both the crystallographic thermal B factors and the observed increase in amide hydrogen exchange kinetics when ferrocytochrome c is oxidized. The relative magnitude of the root mean square volume fluctuations is approximated from an ideal solution treatment of the compressibility data and yields a ratio of delta Vrms (ferri cyt c)/ delta Vrms (ferro cyt c) = 1.3.
Similar articles
-
[Changes in the contractibility of the cytochrome c globule during redox transition].Mol Biol (Mosk). 1986 Mar-Apr;20(2):396-406. Mol Biol (Mosk). 1986. PMID: 3010083 Russian.
-
The conformation of cytochrome c in solution. Localization of a conformational difference between ferri- and ferrocytochrome c on the surface of the molecule.J Biol Chem. 1980 Jul 25;255(14):6694-9. J Biol Chem. 1980. PMID: 6248529
-
Adiabatic compressibility of molten globules.Biochemistry. 1993 Nov 23;32(46):12319-23. doi: 10.1021/bi00097a007. Biochemistry. 1993. PMID: 8241118
-
[Local structure of cytochrome c from horse heart in solution. Conformational analysis using data of two-dimensional nuclear Overhauser effect spectroscopy].Mol Biol (Mosk). 1991 Jan-Feb;25(1):194-204. Mol Biol (Mosk). 1991. PMID: 1654519 Russian.
-
Flexibility of globular proteins in water as revealed by compressibility.Adv Exp Med Biol. 1991;302:753-71. doi: 10.1007/978-1-4899-0664-9_42. Adv Exp Med Biol. 1991. PMID: 1746362 Review.
Cited by
-
Structural analysis of diheme cytochrome c by hydrogen-deuterium exchange mass spectrometry and homology modeling.Biochemistry. 2014 Sep 9;53(35):5619-30. doi: 10.1021/bi500420y. Epub 2014 Aug 27. Biochemistry. 2014. PMID: 25138816 Free PMC article.
-
Adiabatic compressibility of myosin subfragment-1 and heavy meromyosin with or without nucleotide.Biophys J. 1993 Nov;65(5):1899-905. doi: 10.1016/S0006-3495(93)81260-8. Biophys J. 1993. PMID: 8298019 Free PMC article.
-
Interpreting Hydrogen-Deuterium Exchange Events in Proteins Using Atomistic Simulations: Case Studies on Regulators of G-Protein Signaling Proteins.J Phys Chem B. 2018 Oct 11;122(40):9314-9323. doi: 10.1021/acs.jpcb.8b07494. Epub 2018 Oct 1. J Phys Chem B. 2018. PMID: 30222348 Free PMC article.
-
Protein compressibility, dynamics, and pressure.Biophys J. 2000 Jul;79(1):511-25. doi: 10.1016/S0006-3495(00)76313-2. Biophys J. 2000. PMID: 10866977 Free PMC article. Review.
-
Use of metal oxide nanoparticle band gap to develop a predictive paradigm for oxidative stress and acute pulmonary inflammation.ACS Nano. 2012 May 22;6(5):4349-68. doi: 10.1021/nn3010087. Epub 2012 Apr 24. ACS Nano. 2012. PMID: 22502734 Free PMC article.
References
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources