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Recent progress in the electrochemistry of c-type cytochromes
Biochimie, 1994C-type cytochromes are classified into two main groups: i) cytochromes which give fast electrochemical responses at the conventional electrodes in the absence of any promoter (eg multi-heme cytochromes c3); ii) cytochromes which need the presence of promoters or the use of modified electrodes to exhibit fast electrochemical responses (eg one-heme ...
P, Bianco, J, Haladjian
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The biosynthesis of bacterial and plastidic c-type cytochromes
Photosynthesis Research, 1994The biosynthesis of bacterial and plastidic c-type cytochromes includes several steps that occur post-translationally. In the case of bacterial cytochromes, the cytosolically synthesized pre-proteins are translocated across the cytoplasmic membrane, the pre-proteins are cleaved to their mature forms and heme is ligated to the processed apoprotein ...
G, Howe, S, Merchant
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New Perspectives on c-Type Cytochromes
1982Publisher Summary This chapter discusses the various classes of c-type cytochromes, primarily as they occur in nonmitochondrial systems, and their further description as subclasses based on structural relationships observed for purified proteins. The discussion of cytochromes in general is weighted in terms of c-type cytochromes, which present the ...
T E, Meyer, M D, Kamen
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Prospective antibacterial inhibition of c-type cytochrome synthesis
Trends in Molecular Medicine, 2021Sutherland et al. recently reported the in vitro inhibition of Helicobacter hepaticus cytochrome c (cyt c) synthase, which may inactivate c-type cytochromes in this and in other pathogenic bacteria. Here, I discuss the impact of this work, which identifies this conserved synthase as a potential antibacterial target.
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Detection of c-Type Cytochromes Using Enhanced Chemiluminescence
Analytical Biochemistry, 1993A rapid, nontoxic method was devised for staining c-type cytochromes on filters. Bacterial and mitochondrial c-type cytochromes from sodium dodecyl sulfate-polyacrylamide gels were transferred to nitrocellulose filters and visualized by a staining system that relies on their heme peroxidase activity. This involved the use of enhanced chemiluminescence (
Vargas, C., McEwan, A. G., Downie, J. A.
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The Folding Mechanism of c-Type Cytochromes
2010The protein folding field has undoubtedly benefited from studies on the folding mechanism of c-type cytochromes. Many different structural aspects of these small heme-containing proteins led this protein family to be considered a well established model system for such studies.
TRAVAGLINI ALLOCATELLI, Carlo +2 more
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Synthesis of cytochrome c type core from protoporphyrinogen
Biochemical and Biophysical Research Communications, 1964Abstract L-cysteinyl-glycyl-glycyl-L-cysteine has been found to react with protoporphyrinogen to give protoporphyrin-tetrapeptide which has the covalent linkages between the two cysteines and protoporphyrinogen. A new hemopeptide was obtained from the protoporphyrin-tetrapeptide by insertion of iron.
S, Sano, K, Ikeda, S, Sakakibara
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Development and Characteristics of the Euglena C‐Type Cytochromes*
The Journal of Protozoology, 1963SYNOPSIS. Two spectrally different cytochromes, referred to as cytochrome‐552 and ‐556 were isolated from Euglena gracilis (Z) grown under different environmental conditions. Their presence or absence was followed during the dark↔ light adaptation, and their concentrations calculated from spectral data.
J J, WOLKEN, J A, GROSS
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Biogenesis of c-type Cytochromes and Cytochrome Complexes
2009In 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 +6 more
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A systematic investigation of multiheme c-type cytochromes in prokaryotes
JBIC Journal of Biological Inorganic Chemistry, 2010Multiheme c-type cytochromes (MHCs) are metalloproteins that can play various biochemical roles, including enzymatic activity and electron transfer. As electron transfer proteins, the presence of multiple heme cofactors in the vicinity allows electrons to rapidly travel relatively long distances.
SHARMA, SHAILESH +2 more
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