Abstract:
:Cytochromes c require covalent attachment of heme via two thioether bonds at conserved CXXCH motifs, a process accomplished in prokaryotes by eight integral membrane proteins (CcmABCDEFGH), termed System I. Heme is trafficked from inside the cell to outside (via CcmABCD) and chaperoned (holoCcmE) to the cytochrome c synthetase (CcmF/H). Purification of key System I pathway intermediates allowed the determination of heme redox potentials. The data support a model whereby heme is oxidized to form holoCcmE and subsequently reduced by CcmF/H for thioether formation, with Fe(2+) being required for attachment to CXXCH. Results provide insight into mechanisms for the oxidation and reduction of heme in vivo.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Sutherland MC,Rankin JA,Kranz RGdoi
10.1021/acs.biochem.6b00427subject
Has Abstractpub_date
2016-06-07 00:00:00pages
3150-6issue
22eissn
0006-2960issn
1520-4995journal_volume
55pub_type
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