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

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

Biochemistry

journal_title

Biochemistry

authors

Sutherland MC,Rankin JA,Kranz RG

doi

10.1021/acs.biochem.6b00427

subject

Has Abstract

pub_date

2016-06-07 00:00:00

pages

3150-6

issue

22

eissn

0006-2960

issn

1520-4995

journal_volume

55

pub_type

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