Biochemical and Mutational Characterization of the Heme Chaperone CcmE Reveals a Heme Binding Site

CcmE is a heme chaperone that binds heme transiently in the periplasm of Escherichia coli and delivers it to newly synthesized and exported c-type cytochromes. The chemical nature of the covalent bond between heme and H130 is not known. We have purified soluble histidine-tagged CcmE and present its...

Celý popis

Podrobná bibliografie

Vydáno v:	J Bacteriol
Hlavní autoři:	Enggist, Elisabeth, Schneider, Michael J., Schulz, Henk, Thöny-Meyer, Linda
Médium:	Artigo
Jazyk:	Inglês
Vydáno:	American Society for Microbiology (ASM) 2003
Témata:	Enzymes and Proteins
On-line přístup:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC141962/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/12486054/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/JB.185.1.175-183.2003
Tagy:	Přidat tag Žádné tagy, Buďte první, kdo vytvoří štítek k tomuto záznamu!