Structure-function analysis of the heme-binding WWD domain in the bacterial holocytochrome c synthase, CcmFH.

ABSTRACT:

Importance

Heme is an essential co-factor for proteins involved with critical cellular functions, such as energy production and oxygen transport. Thus, understanding how heme interacts with proteins and is moved through cells is a fundamental biological question. This work studies the System I cytochrome c biogenesis pathway, which in some species (including Escherichia coli) is composed of eight integral membrane or membrane-associated proteins called CcmA-H that are proposed to function in two steps to transport and attach heme to apocytochrome c. Cytochrome c requires this heme attachment to function in electron transport chains to generate cellular energy. A conserved WWD heme-handling domain in CcmFH is analyzed and residues critical for heme intera

SUBMITTER: Grunow AL 

PROVIDER: S-EPMC10746174 | biostudies-literature | 2023 Dec

REPOSITORIES: biostudies-literature