scholarly journals Comparing substrate specificity between cytochrome c maturation and cytochrome c heme lyase systems for cytochrome c biogenesis

Metallomics ◽  
2011 ◽  
Vol 3 (4) ◽  
pp. 396 ◽  
Author(s):  
Jesse G. Kleingardner ◽  
Kara L. Bren
Keyword(s):  
Cytochrome C ◽  
Substrate Specificity ◽  
Cytochrome C Maturation ◽  
Cytochrome C Biogenesis ◽  
Cytochrome C Heme Lyase

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

2006 ◽  
Vol 34 (1) ◽  
pp. 150-151 ◽  
Author(s):  
J.W.A. Allen ◽  
S.J. Ferguson
Keyword(s):  
Cytochrome C ◽  
Substrate Specificity ◽  
Nitrogen Cycle ◽  
Covalent Attachment ◽  
Binding Motif ◽  
Gram Negative Bacteria ◽  
Gram Negative ◽  
Cytochrome C Maturation ◽  
Cytochrome C Biogenesis

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. 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; in the present paper, we discuss the substrate specificity of the Ccm apparatus. The main conclusion is that the feature recognized and required in the apocytochrome is simply the two cysteines and the histidine of the haem-binding motif.

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.

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

2009 ◽  
Vol 419 (1) ◽  
pp. 177-186 ◽  
Author(s):  
James W. A. Allen ◽  
Elizabeth B. Sawyer ◽  
Michael L. Ginger ◽  
Paul D. Barker ◽  
Stuart J. Ferguson
Keyword(s):  
Cytochrome C ◽  
Substrate Specificity ◽  
Cysteine Residue ◽  
Covalent Attachment ◽  
Binding Motif ◽  
Post Translational Modification ◽  
Cytochrome C Maturation ◽  
E Coli ◽  
Cytochrome B562 ◽  
Genome Analyses

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 thiol groups of a CXXCH (Cys–Xaa–Xaa–Cys–His) motif. In cells, the haem attachment is an enzyme-catalysed post-translational modification. We have previously shown that co-expression of a variant of Escherichia coli cytochrome b562 containing a CXXCH haem-binding motif with the E. coli Ccm (cytochrome c maturation) proteins resulted in homogeneous maturation of a correctly formed c-type cytochrome. In contrast, in the absence of the Ccm apparatus, the product holocytochrome was heterogeneous, the main species having haem inverted and attached through only one thioether bond. In the present study we use further variants of cytochrome b562 to investigate the substrate specificity of the E. coli Ccm apparatus. The system can mature c-type cytochromes with CCXXCH, CCXCH, CXCCH and CXXCHC motifs, even though these are not found naturally and the extra cysteine residue might, in principle, disrupt the biogenesis proteins which must interact intricately with disulfide-bond oxidizing and reducing proteins in the E. coli periplasm. The Ccm proteins can also attach haem to motifs of the type CXnCH where n ranges from 2 to 6. For n=3 and 4, the haem attachment was correct and homogeneous, but for higher values of n the holocytochromes displayed oxidative addition of sulfur and/or oxygen atoms associated with the covalent haem-attachment process. The implications of our observations for the haem-attachment reaction, for genome analyses and for the substrate specificity of the Ccm system, are discussed.

scholarly journals Role of cytochrome c heme lyase in the import of cytochrome c into mitochondria.

1988 ◽  
Vol 263 (35) ◽  
pp. 19034-19042 ◽  
Author(s):  
D W Nicholson ◽  
C Hergersberg ◽  
W Neupert
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Heme Lyase

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

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
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