Imperial College London

DrDespoinaMavridou

Faculty of Natural SciencesDepartment of Life Sciences

Research Fellow (MRC CDA Fellowship)
 
 
 
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Contact

 

d.mavridou

 
 
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Location

 

1.45Flowers buildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Mavridou:2013:10.1021/bi400398t,
author = {Mavridou, DAI and Clark, MN and Choulat, C and Ferguson, SJ and Stevens, JM},
doi = {10.1021/bi400398t},
journal = {Biochemistry},
pages = {7262--7270},
title = {Probing heme delivery processes in cytochrome c biogenesis System I.},
url = {http://dx.doi.org/10.1021/bi400398t},
volume = {52},
year = {2013}
}

RIS format (EndNote, RefMan)

TY  - JOUR
AB - Cytochromes c comprise a diverse and widespread family of proteins containing covalently bound heme that are central to the life of most organisms. In many bacteria and in certain mitochondria, the synthesis of cytochromes c is performed by a complex post-translational modification apparatus called System I (or cytochrome c maturation, Ccm, system). In Escherichia coli , there are eight maturation proteins, several of which are involved in heme handling, but the mechanism of heme transfer from one protein to the next is not known. Attachment of the heme to the apocytochrome occurs via a novel covalent bond to a histidine residue of the heme chaperone CcmE. The discovery of a variant maturation system (System I) has provided a new tool for studying cytochrome c assembly because the variant CcmE functions via a cysteine residue in the place of the histidine of System I. In this work, we use site-directed mutagenesis on both maturation systems to probe the function of the individual component proteins as well as their concerted action in transferring heme to the cytochrome c substrate. The roles of CcmA, CcmC, CcmE, and CcmF in the heme delivery process are compared between Systems I and I. We show that a previously proposed quinone-binding site on CcmF is not essential for either system. Significant differences in the heme chemistry involved in the formation of cytochromes c in the variant system add new pieces to the cytochrome c biogenesis puzzle.
AU - Mavridou,DAI
AU - Clark,MN
AU - Choulat,C
AU - Ferguson,SJ
AU - Stevens,JM
DO - 10.1021/bi400398t
EP - 7270
PY - 2013///
SP - 7262
TI - Probing heme delivery processes in cytochrome c biogenesis System I.
T2 - Biochemistry
UR - http://dx.doi.org/10.1021/bi400398t
UR - https://www.ncbi.nlm.nih.gov/pubmed/24044352
VL - 52
ER -