AbstractFormation of cytochromes c requires a deceptively simple post-translational modification, the formation of two thioether bonds (or rarely one) between the thiol groups of two cysteine residues found in a CXXCH motif (with some occasional variations) and the vinyl groups of heme. There are three partially characterised systems for facilitating this post-translational modification; within these systems there is also variation. In addition, there are clear indications for two other distinct systems. Here some of the current issues in understanding the systems are analysed
Cytochrome c (cyt c) is a stable protein that functions in a monomeric state as an electron donor fo...
AbstractCytochromes c are metalloproteins that function in electron transfer reactions and contain a...
In vitro formation of Hydrogenobacter thermophilus cytochrome c 552 has previously been demonstrated...
C-type cytochromes are a structurally diverse group of haemoproteins, which are related by the occur...
C-type cytochromes are essential for almost all organisms and are mainly involved in electron transp...
c-type cytochromes are normally characterized by covalent attachment of the iron cofactor haem to pr...
c-type cytochromes are normally characterized by covalent attachment of the iron cofactor haem to pr...
Abstract c-Type cytochromes are characterized by covalent attachment of haem to protein through thio...
AbstractThe reconstitution of biosynthetic pathways from heterologous hosts can help define the mini...
The protein folding field has undoubtedly benefited from studies on the folding mechanism of c-type ...
Cytochromes <i>c</i> comprise a diverse and widespread family of proteins containing covalently boun...
C-type cytochromes are ubiquitous proteins with crucial functions in organisms, which include electr...
: Understanding the role of partially folded intermediate states in the folding mechanism of a prote...
The system I cytochrome c maturation (Ccm) apparatus has been shown to handle a wide variety of apoc...
AbstractCytochromes c are ubiquitous heme proteins that are found in most living organisms and are e...
Cytochrome c (cyt c) is a stable protein that functions in a monomeric state as an electron donor fo...
AbstractCytochromes c are metalloproteins that function in electron transfer reactions and contain a...
In vitro formation of Hydrogenobacter thermophilus cytochrome c 552 has previously been demonstrated...
C-type cytochromes are a structurally diverse group of haemoproteins, which are related by the occur...
C-type cytochromes are essential for almost all organisms and are mainly involved in electron transp...
c-type cytochromes are normally characterized by covalent attachment of the iron cofactor haem to pr...
c-type cytochromes are normally characterized by covalent attachment of the iron cofactor haem to pr...
Abstract c-Type cytochromes are characterized by covalent attachment of haem to protein through thio...
AbstractThe reconstitution of biosynthetic pathways from heterologous hosts can help define the mini...
The protein folding field has undoubtedly benefited from studies on the folding mechanism of c-type ...
Cytochromes <i>c</i> comprise a diverse and widespread family of proteins containing covalently boun...
C-type cytochromes are ubiquitous proteins with crucial functions in organisms, which include electr...
: Understanding the role of partially folded intermediate states in the folding mechanism of a prote...
The system I cytochrome c maturation (Ccm) apparatus has been shown to handle a wide variety of apoc...
AbstractCytochromes c are ubiquitous heme proteins that are found in most living organisms and are e...
Cytochrome c (cyt c) is a stable protein that functions in a monomeric state as an electron donor fo...
AbstractCytochromes c are metalloproteins that function in electron transfer reactions and contain a...
In vitro formation of Hydrogenobacter thermophilus cytochrome c 552 has previously been demonstrated...