Results 231 to 240 of about 42,954 (256)

Cytochrome c Biogenesis

EcoSal Plus, 2008
Escherichia coli employs several c -type cytochromes, which are found in the periplasm or on the periplasmic side of the cytoplasmic membrane; they are used for respiration under different growth conditions. All E. coli c -type cytochromes are multiheme cytochromes;
Julie M, Stevens, Stuart J, Ferguson
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Cytochrome c biogenesis in mitochondria

Mitochondrion, 2008
As part of the respiratory chain, c-type cytochromes are essential electron transporters. They are characterized by the covalent attachment of a heme prosthetic group. The biogenesis of these proteins includes all the processes leading to this fixation. Yeast and animals have evolved a comparatively simple mechanism relying on cytochrome c heme lyases.
P, Giegé, J M, Grienenberger, G, Bonnard   +2 more
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Biogenesis of c-type Cytochromes and Cytochrome Complexes

2009
In most anoxygenic phototrophic bacteria, apocytochromes c are synthesized in the cytoplasm, translocated across the membrane and matured to holocytochromes c on the periplasmic side. The extracytoplasmic maturation process requires a complex biogenesis pathway (Ccm-system I) consisting of up to ten components to carry out specific steps. These include
Sanders, Carsten, Turkarslan, Serdar, Önder, Özlem, Frawley, Elaine R., Kranz, Robert G., Koch, Hans-Georg, Daldal, Fevzi   +6 more
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Redox Processes Controlling the Biogenesis of c -Type Cytochromes

Antioxidants & Redox Signaling, 2010
In mitochondria, two mono heme c-type cytochromes are essential electron shuttles of the respiratory chain. They are characterized by the covalent attachment of their heme C to a CXXCH motif in the apoproteins. This post-translational modification occurs in the intermembrane space compartment.
Bonnard, G., Corvest, V., Meyer, E.H., Hamel, P.P.   +3 more
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FDX1 Is Required for the Biogenesis of Mitochondrial Cytochrome c Oxidase in Mammalian Cells

Journal of Molecular Biology, 2023
Ferredoxins (FDXs) are evolutionarily conserved iron-sulfur (Fe-S) proteins that function as electron transfer proteins in diverse metabolic pathways. Mammalian mitochondria contain two ferredoxins, FDX1 and FDX2, which share a high degree of structural similarity but exhibit different functionalities.
Mohammad Zulkifli, Adriana U. Okonkwo, Vishal M. Gohil   +2 more
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Covalent cofactor attachment to proteins: cytochrome c biogenesis

Biochemical Society Transactions, 2005
Haem (Fe-protoporphyrin IX) is a cofactor found in a wide variety of proteins. It confers diverse functions, including electron transfer, the binding and sensing of gases, and many types of catalysis. The majority of cofactors are non-covalently attached to proteins.
J M, Stevens, T, Uchida, O, Daltrop, S J, Ferguson   +3 more
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Complexity and diversity in c-type cytochrome biogenesis systems

Biochemical Society Transactions, 2005
c-type cytochromes contain haem covalently attached to protein by thioether bonds formed post-translationally and requiring a dedicated biogenesis apparatus. Three biogenesis systems, found in different cell types, are well known. Here we discuss emerging evidence for at least one additional system, for unanticipated diversity in the location of the ...
J W A, Allen, M L, Ginger, S J, Ferguson
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Recombinant Biogenesis and Analysis of Cytochrome c Species

Recombinant expression and biogenesis of cytochrome c species is a simple and efficient method for the production of holocytochrome c species, thus presenting an avenue for the study of cytochrome c or the cytochrome c biogenesis pathways responsible for heme attachment. Here, we describe a method for recombinant E.
Alicia N. Kreiman, Tania Yeasmin, Molly C. Sutherland   +2 more
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Biogenesis of Yeast Mitochondrial Cytochrome c: A Unique Relationship to the TOM Machinery

Journal of Molecular Biology, 2003
The import of cytochrome c into the mitochondrial intermembrane space is not understood at a mechanistic level. While the precursor apocytochrome c can insert into protein-free lipid bilayers, the purified translocase of the outer membrane (TOM) complex supports the translocation of apocytochrome c into proteoliposomes.
Wiedemann, Nils, Kozjak-Pavlovic, Vera, Prinz, Thorsten, Ryan, Michael T., Meisinger, Chris, Pfanner, Nikolaus, Truscott, Kaye N.   +6 more
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Avoidance of the cytochrome c biogenesis system by periplasmic CXXCH motifs

Biochemical Society Transactions, 2008
The CXXCH motif is usually recognized in the bacterial periplasm as a haem attachment site in apocytochromes c. There is evidence that the Escherichia coli Ccm (cytochrome c maturation) system recognizes little more than the CXXCH sequence. A limited number of periplasmic proteins have this motif and yet are not c-type cytochromes.
Despoina A I, Mavridou, Martin, Braun, Linda, Thöny-Meyer, Julie M, Stevens, Stuart J, Ferguson   +4 more
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