Abstract 1549 Heme reduction in CcmFH, a key enzyme within the bacterial System I cytochrome c biogenesis pathway

Cytochromes c possess diverse and often critical functions in prokaryotes, ranging from respiration and detoxification to noncanonical functions (e.g., iron uptake, extracellular nanowires). This protein is a model for post-translational modification as all cytochromes c require the covalent attachment of heme to a conserved CXXCH motif to properly fold and function. Despite the diversity of cytochromes c, all cytochrome c biogenesis (i.e. covalent heme attachment) is performed by one of three pathways called System I (prokaryotes), System II (prokaryotes) or System III (eukaryotes).

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Publication Details

Journal
Journal of Biological Chemistry
Published
2025-05-01
DOI
https://doi.org/10.1016/j.jbc.2025.109600
Primary Topic
Cancer, Hypoxia, and Metabolism
Type
article
Field-Weighted Citation Impact
0.00
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article

Abstract 1549 Heme reduction in CcmFH, a key enzyme within the bacterial System I cytochrome c biogenesis pathway

Molly C. Sutherland, Robert G. Kranz, Allison Mattern
Journal of Biological Chemistry
Cancer, Hypoxia, and Metabolism
article

Abstract 1549 Heme reduction in CcmFH, a key enzyme within the bacterial System I cytochrome c biogenesis pathway

Molly C. Sutherland, Robert G. Kranz, Allison Mattern
article en

Abstract

Cytochromes c possess diverse and often critical functions in prokaryotes, ranging from respiration and detoxification to noncanonical functions (e.g., iron uptake, extracellular nanowires). This protein is a model for post-translational modification as all cytochromes c require the covalent attachment of heme to a conserved CXXCH motif to properly fold and function. Despite the diversity of cytochromes c, all cytochrome c biogenesis (i.e. covalent heme attachment) is performed by one of three pathways called System I (prokaryotes), System II (prokaryotes) or System III (eukaryotes).

Journal of Biological ChemistryVol. 301(5)
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Cancer, Hypoxia, and Metabolism
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