Results 1 to 10 of about 11,485 (176)

Bacterial TANGO2 homologs are heme-trafficking proteins that facilitate biosynthesis of cytochromes c. [PDF]

open access: yesmBio, 2023
Heme, an essential molecule for virtually all living organisms, acts primarily as a cofactor in a large number of proteins. However, how heme is mobilized from the site of synthesis to the locations where hemoproteins are assembled remains largely ...
Han S, Guo K, Wang W, Tao YJ, Gao H.
europepmc   +4 more sources

Like iron in the blood of the people: the requirement for heme trafficking in iron metabolism. [PDF]

open access: yesFront Pharmacol, 2014
Heme is an iron-containing porphyrin ring that serves as a prosthetic group in proteins that function in diverse metabolic pathways. Heme is also a major source of bioavailable iron in the human diet.
Korolnek T, Hamza I.
europepmc   +5 more sources

Analysis of putative heme ligands in the System I bacterial cytochrome <i>c</i> biogenesis heme transporter, CcmCD. [PDF]

open access: yesMicrobiol Spectr
Heme is a key co-factor for biologically important proteins that are required for critical cellular functions such as oxygen transport and energy production.
Kreiman AN   +5 more
europepmc   +2 more sources

Inhibitors of cytochrome <i>c</i> biogenesis pathways. [PDF]

open access: yesmBio
The unique composition of bacterial electron transport chains (ETCs), distinct from the human mitochondrial ETC, presents opportunities for selective antibacterial targeting.
Mendez DL   +8 more
europepmc   +2 more sources

Notes from the Underground: Heme Homeostasis in C. elegans

open access: yesBiomolecules, 2023
Heme is an iron-containing tetrapyrrole that plays a critical role in various biological processes, including oxygen transport, electron transport, signal transduction, and catalysis.
Caiyong Chen, Iqbal Hamza
doaj   +1 more source

In Campylobacter jejuni, a new type of chaperone receives heme from ferrochelatase

open access: yesFrontiers in Genetics, 2023
Intracellular heme formation and trafficking are fundamental processes in living organisms. Bacteria and archaea utilize three biogenesis pathways to produce iron protoporphyrin IX (heme b) that diverge after the formation of the common intermediate ...
Jordi Zamarreño Beas   +6 more
doaj   +1 more source

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

open access: yesmBio, 2023
Heme trafficking is a fundamental biological process, yet its direct study has been hampered due to heme’s tight intracellular regulation, heme cytotoxicity, and the transient nature of trafficking.
Amber L. Grunow   +3 more
doaj   +1 more source

Ferrochelatase: Mapping the Intersection of Iron and Porphyrin Metabolism in the Mitochondria

open access: yesFrontiers in Cell and Developmental Biology, 2022
Porphyrin and iron are ubiquitous and essential for sustaining life in virtually all living organisms. Unlike iron, which exists in many forms, porphyrin macrocycles are mostly functional as metal complexes. The iron-containing porphyrin, heme, serves as
Chibuike David Obi   +5 more
doaj   +1 more source

Ferric reductase-related proteins mediate fungal heme acquisition

open access: yeseLife, 2022
Heme can serve as iron source in many environments, including the iron-poor animal host environment. The fungal pathobiont Candida albicans expresses a family of extracellular CFEM hemophores that capture heme from host proteins and transfer it across ...
Udita Roy   +6 more
doaj   +1 more source

Structures of the CcmABCD heme release complex at multiple states

open access: yesNature Communications, 2022
Bacterial ABC transporter complex CcmABCD, a part of cytochrome c maturation system, transfers heme from one binding partner (CcmC) to another (CcmE). Here authors describe high resolution cryo-EM structures of CcmABCD in multiple states and propose a ...
Jiao Li   +14 more
doaj   +1 more source

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