Tethered heme domains in a triheme cytochrome allow for increased electron transport distances.

ABSTRACT: Decades of research describe myriad redox enzymes that contain cofactors arranged in tightly packed chains facilitating rapid and controlled intra-protein electron transfer. Many such enzymes participate in extracellular electron transfer (EET), a process which allows microorganisms to conserve energy in anoxic environments by exploiting mineral oxides and other extracellular substrates as terminal electron acceptors. In this work, we describe the properties of the triheme cytochrome PgcA from Geobacter sulfurreducens. PgcA has been shown to play an important role in EET but is unusual in containing three CXXCH heme binding motifs that are separated by repeated (PT)_x motifs, suggested to enhance binding to mineral surfaces. Using a combination of structural, electrochemical, and

SUBMITTER: Nash BW 

PROVIDER: S-EPMC11520253 | biostudies-literature | 2024 Nov

REPOSITORIES: biostudies-literature