Thermodynamic properties of triheme cytochrome PpcF from Geobacter metallireducens reveal unprecedented functional mechanism.
The bacterium Geobacter metallireducens is highly efficient in long-range extracellular electron transfer, a process that relies on an efficient bridging between the cytoplasmic electron donors and the extracellular acceptors. The periplasmic triheme cytochromes are crucial players in these processes and thus the understanding of their functional mechanism is crucial to elucidate the extracellular electron transfer processes in this microorganism. The triheme cytochrome PpcF from G. metallireducens has the lowest amino acid sequence identity with the remaining cytochromes from the PpcA-family of G. sulfurreducens and G. metallireducens, making it an interesting target for structural and functional studies. In this work, we performed a detailed functional and thermodynamic characterization of cytochrome PpcF by the complementary usage of NMR and visible spectroscopic techniques. The results obtained show that the heme reduction potentials are negative, different from each other and are also modulated by the redox and redox-Bohr interactions that assure unprecedented mechanistic features to the protein. The results showed that the order of oxidation of the hemes in cytochrome PpcF is maintained in the entire physiological pH range. The considerable separation of the hemes' redox potential values facilitates a sequential transfer within the chain of redox centers in PpcF, thus assuring electron transfer directionality to the electron acceptors.
['Ferreira|Marisa R|MR|', 'Fernandes|Tomás M|TM|', 'Salgueiro|Carlos A|CA|']
D001426:Bacterial Proteins D003580:Cytochromes D045302:Geobacter D006418:Heme D006863:Hydrogen-Ion Concentration D009682:Magnetic Resonance Spectroscopy D019906:Nuclear Magnetic Resonance, Biomolecular D010084:Oxidation-Reduction D013816:Thermodynamics
Geobacter Electron transfer NMR Multiheme cytochromes Redox characterization