Abstract
In this article, we review a microstate model that uses protonation and redox microstates in order to understand the complex pH and redox titration of proteins and other polyelectrolytes. From this model, it becomes obvious that it is impossible to assign pKa values or redox potentials to individual protonatable or redox-active sites in a protein in which many of such sites interact. Instead each site is associated with many microscopic equilibrium constants that may lead to irregular or even non-monotonic titration curves of some groups. The microstate model provides a closed theoretical framework to discuss such phenomena.
Received: 2012-11-17
Accepted: 2013-1-21
Published Online: 2013-01-28
Published in Print: 2013-05-01
©2013 by Walter de Gruyter Berlin Boston
You are currently not able to access this content.
You are currently not able to access this content.
Articles in the same Issue
- Masthead
- Masthead
- Guest Editorial
- Highlight: European BioEnergetics Conference 2012 in Freiburg
- Highlight: European Bioenergetics Conference 2012 in Freiburg
- Structure of caa3 cytochrome c oxidase – a nature-made enzyme-substrate complex
- Recent advances in the electrochemistry and spectroelectrochemistry of membrane proteins
- pKa values and redox potentials of proteins. What do they mean?
- Cyclophilin D as a potential target for antioxidants in neurodegeneration: the X-ALD case
- A critical appraisal of the role of respiratory supercomplexes in mitochondria
- Mechanistic aspects of sodium-binding sites in LeuT-like fold symporters
- Hydroxynonenal-stimulated activity of the uncoupling protein in Acanthamoeba castellanii mitochondria under phosphorylating conditions
- The antiporter-like subunit constituent of the universal adaptor of complex I, group 4 membrane-bound [NiFe]-hydrogenases and related complexes
- Alternate pathways for NADH oxidation in Thermus thermophilus using type 2 NADH dehydrogenases
- A new trend in the complex I research field
- Research Articles/Short Communications
- Protein Structure and Function
- Expression in non-melanogenic systems and purification of soluble variants of human tyrosinase
- Chemical and enzymatic characterization of recombinant rabbit muscle pyruvate kinase
Keywords for this article
microstate model;
pH titration;
proteins;
protonation;
redox potentials
Articles in the same Issue
- Masthead
- Masthead
- Guest Editorial
- Highlight: European BioEnergetics Conference 2012 in Freiburg
- Highlight: European Bioenergetics Conference 2012 in Freiburg
- Structure of caa3 cytochrome c oxidase – a nature-made enzyme-substrate complex
- Recent advances in the electrochemistry and spectroelectrochemistry of membrane proteins
- pKa values and redox potentials of proteins. What do they mean?
- Cyclophilin D as a potential target for antioxidants in neurodegeneration: the X-ALD case
- A critical appraisal of the role of respiratory supercomplexes in mitochondria
- Mechanistic aspects of sodium-binding sites in LeuT-like fold symporters
- Hydroxynonenal-stimulated activity of the uncoupling protein in Acanthamoeba castellanii mitochondria under phosphorylating conditions
- The antiporter-like subunit constituent of the universal adaptor of complex I, group 4 membrane-bound [NiFe]-hydrogenases and related complexes
- Alternate pathways for NADH oxidation in Thermus thermophilus using type 2 NADH dehydrogenases
- A new trend in the complex I research field
- Research Articles/Short Communications
- Protein Structure and Function
- Expression in non-melanogenic systems and purification of soluble variants of human tyrosinase
- Chemical and enzymatic characterization of recombinant rabbit muscle pyruvate kinase