[HTML][HTML] Investigation of the Molecular Mechanisms of the Eukaryotic Cytochrome-c Maturation System

AV Silva, MO Firmino, NL Costa, RO Louro… - Biomolecules, 2022 - mdpi.com
Cytochromes-c are ubiquitous heme proteins with enormous impact at the cellular level,
being key players in metabolic processes such as electron transfer chains and apoptosis …

What is the substrate specificity of the System I cytochrome c biogenesis apparatus?

JWA Allen, SJ Ferguson - Biochemical Society Transactions, 2006 - portlandpress.com
c-Type cytochromes are characterized by covalent attachment of haem to protein through
thioether bonds between the vinyl groups of the haem and the thiols of a CXXCH motif …

Variant c-type cytochromes as probes of the substrate specificity of the E. coli cytochrome c maturation (Ccm) apparatus

JWA Allen, EB Sawyer, ML Ginger… - Biochemical …, 2009 - portlandpress.com
c-type cytochromes are normally characterized by covalent attachment of the iron cofactor
haem to protein through two thioether bonds between the vinyl groups of the haem and the …

Variation of the axial haem ligands and haem-binding motif as a probe of the Escherichia coli c-type cytochrome maturation (Ccm) system

JWA Allen, SJ Ferguson - Biochemical Journal, 2003 - portlandpress.com
Cytochromes c are typically characterized by the covalent attachment of haem to
polypeptide through two thioether bonds with the cysteine residues of a Cys-Xaa-Xaa-Cys …

Cytochrome c biogenesis in bacteria: a possible pathway begins to emerge

L Thöny‐Meyer, D Ritz, H Hennecke - Molecular microbiology, 1994 - Wiley Online Library
Cytochrome c biogenesis describes the posttranslational pathway for the conversion of pre‐
apocytochrome c into the mature holocytochrome c. It involves an unknown number of …

The histidine of the c-type cytochrome CXXCH haem-binding motif is essential for haem attachment by the Escherichia coli cytochrome c maturation (Ccm) …

JWA Allen, N Leach, SJ Ferguson - Biochemical Journal, 2005 - portlandpress.com
c-type cytochromes are characterized by covalent attachment of haem to the protein by two
thioether bonds formed between the haem vinyl groups and the cysteine sulphurs in a …

[HTML][HTML] Loss of either of the two heme-binding cysteines from a class I c-type cytochrome has a surprisingly small effect on physicochemical properties

EJ Tomlinson, SJ Ferguson - Journal of Biological Chemistry, 2000 - ASBMB
Almost without exception, c-type cytochromes have heme covalently attached via two
thioether linkages to the cysteine residues of a CXXCH motif. The reasons for the covalent …

Cytochrome c biogenesis System I

JM Stevens, DAI Mavridou, R Hamer… - The FEBS …, 2011 - Wiley Online Library
Cytochromes c are widespread respiratory proteins characterized by the covalent
attachment of heme. The formation of c‐type cytochromes requires, in all but a few …

A stable, molten-globule-like cytochrome c

P Wittung-Stafshede - Biochimica et Biophysica Acta (BBA)-Protein …, 1998 - Elsevier
Expression of cytochrome c from Thermus thermophilus in Escherichia coli (E. coli) leads to
a protein with characteristics of a molten globule. Unfolding induced by guanidine …

[HTML][HTML] A variant System I for cytochrome c biogenesis in archaea and some bacteria has a novel CcmE and no CcmH

JWA Allen, EM Harvat, JM Stevens, SJ Ferguson - FEBS letters, 2006 - Elsevier
C-type cytochromes are characterized by post-translational covalent attachment of heme to
thiols that occur in a Cys-Xxx-Xxx-Cys-His motif. Three distinct biogenesis systems are …