A new research study from the Biochemistry & Bioenergetics of Heme Proteins Lab at UCIBIO-NOVA, led by Carlos A. Salgueiro, reveals unique features of a multiheme cytochrome.
The research work “Thermodynamic properties of triheme cytochrome PpcF from Geobacter metallireducens reveal unprecedented functional mechanism” has just been published in the BBA – Bioenergetics Journal.
Marisa R. Ferreira and Tomás M. Fernandes, PhD students at the Biochemistry & Bioenergetics of Heme Proteins Lab, studied the redox properties and functional mechanisms of PpcF, a periplasmic cytochrome from Geobacter metallireducens proposed to be involved in nitrate respiration by exchanging electrons with the nitrate reductase enzyme. The results obtained “show that the way PpcF is designed warrants an important directionality for electron transfer along the cytochrome’s heme redox chain and to the final electron acceptor. These properties are unique amongst other known multiheme cytochromes”, explained Marisa Ferreira and Tomás Fernandes.
This work is another step in the understanding of the molecular mechanisms of extracellular electron transfer in Geobacter. Also, the results obtained can be combined with structural information and further used to rationally design mutants that may improve the bioremediation and bioenergy production capabilities of the host bacterium.
Article
Biochimica et Biophysica Acta - Bioenergetics
Marisa R.Ferreira, Tomás M.Fernandes and Carlos A.Salgueiro