Characterization of recombinant horse cytochrome c synthesized with the assistance of Escherichia coli cytochrome c maturation factors

2002 ◽  
Vol 1601 (2) ◽  
pp. 215-221 ◽  
Author(s):  
Jason A. Kellogg ◽  
Kara L. Bren
Keyword(s):  
Escherichia Coli ◽  
Cytochrome C ◽  
Cytochrome C Maturation ◽  
Horse Cytochrome

Characterization of Horse Cytochrome c Expressed in Escherichia coli

2001 ◽  
Vol 22 (2) ◽  
pp. 220-224 ◽  
Author(s):  
Chetan N. Patel ◽  
Maria C. Lind ◽  
Gary J. Pielak
Keyword(s):  
Escherichia Coli ◽  
Cytochrome C ◽  
Horse Cytochrome

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

2003 ◽  
Vol 375 (3) ◽  
pp. 721-728 ◽  
Author(s):  
James W. A. ALLEN ◽  
Stuart J. FERGUSON
Keyword(s):  
Escherichia Coli ◽  
Cytochrome C ◽  
Covalent Attachment ◽  
Binding Motif ◽  
Cytochrome C Maturation ◽  
Cytochromes C ◽  
Cytochrome C552 ◽  
Haem Iron ◽  
Made In ◽  
Uncatalysed Reaction

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-His peptide motif. In many Gram-negative bacteria, the haem is attached to the polypeptide by the periplasmically functioning cytochrome c maturation (Ccm) proteins. Exceptionally, Hydrogenobacter thermophilus cytochrome c552 can be expressed as a stable holocytochrome both in the cytoplasm of Escherichia coli in an apparently uncatalysed reaction and also in the periplasm in a Ccm-mediated reaction. In the present study we show that a Met60→Ala variant of c552, which does not have the usual distal methionine ligand to the haem iron of the mature cytochrome, can be made in the periplasm by the Ccm system. However, no holocytochrome could be detected when this variant was expressed cytoplasmically. These data highlight differences between the two modes of cytochrome c assembly. In addition, we report investigations of haem attachment to cytochromes altered to have the special Cys-Trp-Ser-Cys-Lys haem-binding motif, and Cys-Trp-Ser-Cys-His and Cys-Trp-Ala-Cys-His analogues, of the active-site haem of nitrite reductase NrfA.

The Escherichia coli cytochrome c maturation (Ccm) apparatus can mature cytochromes with an extra cysteine within or adjacent to the CXXCH motif

2006 ◽  
Vol 34 (1) ◽  
pp. 91-93 ◽  
Author(s):  
J.W.A. Allen ◽  
S.J. Ferguson
Keyword(s):  
Escherichia Coli ◽  
Cytochrome C ◽  
Nitrogen Cycle ◽  
Covalent Attachment ◽  
Gram Negative Bacteria ◽  
Gram Negative ◽  
Cytochrome C Maturation ◽  
Free Thiol ◽  
Haem Iron

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 Cys-Xaa-Xaa-Cys-His motif. Proteins of this type play crucial roles in the biochemistry of the nitrogen cycle. Many Gram-negative bacteria use the Ccm (cytochrome c maturation) proteins for the post-translational haem attachment to their c-type cytochromes. The Ccm system can correctly mature c-type cytochromes with CCXXCH, CCXCH, CXCCH and CXXCHC motifs, even though these are not found naturally and the extra cysteine might, in principle, disrupt the biogenesis proteins. The non-occurrence of these motifs probably relates to the destructive chemistry that can occur if a free thiol reacts with haem iron to generate a radical.

Nanoscopic and Redox Characterization of Engineered Horse Cytochrome c Chemisorbed on a Bare Gold Electrode

2007 ◽  
Vol 26 (4) ◽  
pp. 271-279 ◽  
Author(s):  
Laura Andolfi ◽  
Paola Caroppi ◽  
Anna Rita Bizzarri ◽  
Maria Cristina Piro ◽  
Federica Sinibaldi ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Gold Electrode ◽  
Bare Gold Electrode ◽  
Horse Cytochrome ◽  
Bare Gold
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