Structure and redox properties of the diheme electron carrier cytochrome c₄ from Pseudomonas aeruginosa.

ABSTRACT: At low oxygen concentrations, respiration of Pseudomonas aeruginosa (Pa) and other bacteria relies on activity of cytochrome cbb₃ oxidases. A diheme cytochrome c₄ (cyt c₄) donates electrons to Pa cbb₃ oxidases to enable oxygen reduction and proton pumping by these enzymes. Given the importance of this redox pathway for bacterial pathogenesis, both cyt c₄ and cbb₃ oxidase are potential targets for new antibacterial strategies. The structural information about these two proteins, however, is scarce, and functional insights for Pa and other bacteria have been primarily drawn from analyses of the analogous system from Pseudomonas stutzeri (Ps). Herein, we describe characterization of structural and redox properties of cyt c

SUBMITTER: Carpenter JM 

PROVIDER: S-EPMC7480007 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature