Imperial College London


Faculty of Natural SciencesDepartment of Life Sciences

Research Fellow (MRC CDA Fellowship)







1.45Flowers buildingSouth Kensington Campus






BibTex format

author = {Mavridou, DAI and Stevens, JM and Mönkemeyer, L and Daltrop, O and di, Gleria K and Kessler, BM and Ferguson, SJ and Allen, JWA},
doi = {10.1074/jbc.M111.313692},
journal = {J Biol Chem},
pages = {2342--2352},
title = {A pivotal heme-transfer reaction intermediate in cytochrome c biogenesis.},
url = {},
volume = {287},
year = {2012}

RIS format (EndNote, RefMan)

AB - c-Type cytochromes are widespread proteins, fundamental for respiration or photosynthesis in most cells. They contain heme covalently bound to protein in a highly conserved, highly stereospecific post-translational modification. In many bacteria, mitochondria, and archaea this heme attachment is catalyzed by the cytochrome c maturation (Ccm) proteins. Here we identify and characterize a covalent, ternary complex between the heme chaperone CcmE, heme, and cytochrome c. Formation of the complex from holo-CcmE occurs in vivo and in vitro and involves the specific heme-binding residues of both CcmE and apocytochrome c. The enhancement and attenuation of the amounts of this complex correlates completely with known consequences of mutations in genes for other Ccm proteins. We propose the complex is a trapped catalytic intermediate in the cytochrome c biogenesis process, at the point of heme transfer from CcmE to the cytochrome, the key step in the maturation pathway.
AU - Mavridou,DAI
AU - Stevens,JM
AU - Mönkemeyer,L
AU - Daltrop,O
AU - di,Gleria K
AU - Kessler,BM
AU - Ferguson,SJ
AU - Allen,JWA
DO - 10.1074/jbc.M111.313692
EP - 2352
PY - 2012///
SP - 2342
TI - A pivotal heme-transfer reaction intermediate in cytochrome c biogenesis.
T2 - J Biol Chem
UR -
UR -
VL - 287
ER -