scholarly journals Heme Trafficking and Modifications during System I Cytochrome c Biogenesis: Insights from Heme Redox Potentials of Ccm Proteins

Biochemistry ◽  
2016 ◽  
Vol 55 (22) ◽  
pp. 3150-3156 ◽  
Author(s):  
Molly C. Sutherland ◽  
Joel A. Rankin ◽  
Robert G. Kranz
Keyword(s):  
Cytochrome C ◽  
Redox Potentials ◽  
Cytochrome C Biogenesis ◽  
Heme Trafficking

scholarly journals HEME Trafficking by the Cytochrome C Biogenesis Pathways

2018 ◽  
Vol 114 (3) ◽  
pp. 425a
Author(s):  
Molly C. Sutherland ◽  
Joshua M. Jarodsky ◽  
Robert G. Kranz
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Biogenesis ◽  
Heme Trafficking

scholarly journals Heme Trafficking by the Cytochrome C Biogenesis Pathways

2017 ◽  
Vol 112 (3) ◽  
pp. 65a-66a
Author(s):  
Molly C. Sutherland ◽  
Joel A. Rankin ◽  
Robert G. Kranz
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Biogenesis ◽  
Heme Trafficking

ABC transporters associated with cytochrome c biogenesis

2001 ◽  
Vol 152 (3-4) ◽  
pp. 323-329 ◽  
Author(s):  
Barry S Goldman ◽  
Robert G Kranz
Keyword(s):  
Cytochrome C ◽  
Abc Transporters ◽  
Cytochrome C Biogenesis

Avoidance of the cytochrome c biogenesis system by periplasmic CXXCH motifs

2008 ◽  
Vol 36 (6) ◽  
pp. 1124-1128 ◽  
Author(s):  
Despoina A.I. Mavridou ◽  
Martin Braun ◽  
Linda Thöny-Meyer ◽  
Julie M. Stevens ◽  
Stuart J. Ferguson
Keyword(s):  
Cytochrome C ◽  
Tertiary Structure ◽  
Evolutionary Relationship ◽  
Attachment Site ◽  
Cytochrome C Maturation ◽  
E Coli ◽  
Cytochrome C Biogenesis ◽  
Periplasmic Proteins ◽  
Bona Fide

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. To explore how unwanted haem attachment to CXXCH might be avoided, and to determine whether haem attachment to the surface of a non-cytochrome protein would be possible, we converted the active-site CXXCK motif of a thioredoxin-like protein into CXXCH, the C-terminal domain of the transmembrane oxidoreductase DsbD (cDsbD). The E. coli Ccm system was found to catalyse haem attachment to a very small percentage of the resultant protein (∼0.2%). We argue that cDsbD folds sufficiently rapidly that only a small fraction fails to avoid the Ccm system, in contrast with bona fide c-type cytochromes that only adopt their tertiary structure following haem attachment. We also demonstrate covalent haem attachment at a low level in vivo to the periplasmic disulfide isomerase DsbC, which contains a native CXXCH motif. These observations provide insight into substrate recognition by the Ccm system and expand our understanding of the requirements for covalent haem attachment to proteins. The possible evolutionary relationship between thioredoxins and c-type cytochromes is discussed.

Molecular and immunological analysis of an ABC transporter complex required for cytochrome c biogenesis

1997 ◽  
Vol 268 (4) ◽  
pp. 724-738 ◽  
Author(s):  
Barry S. Goldman ◽  
Diana L. Beckman ◽  
Anil Bali ◽  
Elizabeth M. Monika ◽  
Karen K. Gabbert ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Abc Transporter ◽  
Immunological Analysis ◽  
Cytochrome C Biogenesis

scholarly journals The CcmC:Heme:CcmE Complex in Heme Trafficking and Cytochrome c Biosynthesis

2010 ◽  
Vol 401 (3) ◽  
pp. 350-362 ◽  
Author(s):  
Cynthia Richard-Fogal ◽  
Robert G. Kranz
Keyword(s):  
Cytochrome C ◽  
Heme Trafficking
Sign in / Sign up

Export Citation Format

Share Document