Cytochrome c6 is a soluble heme protein that serves as a photosynthetic electron transport component in cyanobacteria and algae, carrying electrons from the cytochrome bf complex to photosystem I. The rapid accumulation of cytochrome c6 sequence data from a wide range of species, combined with significant advances in determining high resolution three-dimensional structures, provides a powerful database for investigating the relationship between structure and function. The fact that the gene encoding cytochrome c6 can be readily modified in a number of species adds to the usefulness of cytochrome c6 as a tool for comparative analysis. Efforts to relate cytochrome c6 sequence information to structure, and structural information to function depend on knowledge of the physical and thermodynamic properties of the cytochrome from different species. To this end we have determined the optical extinction coefficient, the oxidation/reduction midpoint potential, and the pH dependence of the midpoint potential of cytochrome c6 isolated from three cyanobacteria, Arthrospira maxima, Microcystis aeruginosa, and Synechocystis 6803. Copyright (C) 1999 Elsevier Science B.V.
|Number of pages||6|
|Journal||Biochimica et Biophysica Acta - Bioenergetics|
|State||Published - Oct 6 1999|
Copyright 2007 Elsevier B.V., All rights reserved.
- Extinction coefficient
- Optical spectroscopy
- Redox potentiometry
ASJC Scopus subject areas
- Cell Biology