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Title: A Copper Relay System Involving Two Periplasmic Chaperones Drives cbb3-Type Cytochrome c Oxidase Biogenesis in Rhodobacter capsulatus

Abstract

PccA and SenC are periplasmic copper chaperones required for the biogenesis of cbb3-type cytochrome c oxidase (cbb3-Cox) in Rhodobacter capsulatus at physiological Cu concentrations. However, both proteins are dispensable for cbb3-Cox assembly when the external Cu concentration is high. PccA and SenC bind Cu using Met and His residues and Cys and His residues as ligands, respectively, and both proteins form a complex during cbb3-Cox biogenesis. SenC also interacts directly with cbb3-Cox, as shown by chemical cross-linking. Here we determined the periplasmic concentrations of both proteins in vivo and analyzed their Cu binding stoichiometries and their Cu(I) and Cu(II) binding affinity constants (KD) in vitro. Our data show that both proteins bind a single Cu atom with high affinity. In vitro Cu transfer assays demonstrate Cu transfer both from PccA to SenC and from SenC to PccA at similar levels. We conclude that PccA and SenC constitute a Cu relay system that facilitates Cu delivery to cbb3-Cox.

Authors:
 [1];  [2];  [2];  [2];  [3];  [3];  [3]; ORCiD logo [2]
  1. Univ. of Pennsylvania, Philadelphia, PA (United States); Univ. of Freiburg (Germany)
  2. Univ. of Freiburg (Germany)
  3. Univ. of Pennsylvania, Philadelphia, PA (United States)
Publication Date:
Research Org.:
Univ. of Pennsylvania, Philadelphia, PA (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES)
OSTI Identifier:
1546085
Grant/Contract Number:  
FG02-91ER20052
Resource Type:
Accepted Manuscript
Journal Name:
ACS Chemical Biology
Additional Journal Information:
Journal Volume: 13; Journal Issue: 5; Journal ID: ISSN 1554-8929
Publisher:
American Chemical Society (ACS)
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES

Citation Formats

Trasnea, Petru-Iulian, Andrei, Andreea, Marckmann, Dorian, Utz, Marcel, Khalfaoui-Hassani, Bahia, Selamoglu, Nur, Daldal, Fevzi, and Koch, Hans-Georg. A Copper Relay System Involving Two Periplasmic Chaperones Drives cbb3-Type Cytochrome c Oxidase Biogenesis in Rhodobacter capsulatus. United States: N. p., 2018. Web. doi:10.1021/acschembio.8b00293.
Trasnea, Petru-Iulian, Andrei, Andreea, Marckmann, Dorian, Utz, Marcel, Khalfaoui-Hassani, Bahia, Selamoglu, Nur, Daldal, Fevzi, & Koch, Hans-Georg. A Copper Relay System Involving Two Periplasmic Chaperones Drives cbb3-Type Cytochrome c Oxidase Biogenesis in Rhodobacter capsulatus. United States. https://doi.org/10.1021/acschembio.8b00293
Trasnea, Petru-Iulian, Andrei, Andreea, Marckmann, Dorian, Utz, Marcel, Khalfaoui-Hassani, Bahia, Selamoglu, Nur, Daldal, Fevzi, and Koch, Hans-Georg. Tue . "A Copper Relay System Involving Two Periplasmic Chaperones Drives cbb3-Type Cytochrome c Oxidase Biogenesis in Rhodobacter capsulatus". United States. https://doi.org/10.1021/acschembio.8b00293. https://www.osti.gov/servlets/purl/1546085.
@article{osti_1546085,
title = {A Copper Relay System Involving Two Periplasmic Chaperones Drives cbb3-Type Cytochrome c Oxidase Biogenesis in Rhodobacter capsulatus},
author = {Trasnea, Petru-Iulian and Andrei, Andreea and Marckmann, Dorian and Utz, Marcel and Khalfaoui-Hassani, Bahia and Selamoglu, Nur and Daldal, Fevzi and Koch, Hans-Georg},
abstractNote = {PccA and SenC are periplasmic copper chaperones required for the biogenesis of cbb3-type cytochrome c oxidase (cbb3-Cox) in Rhodobacter capsulatus at physiological Cu concentrations. However, both proteins are dispensable for cbb3-Cox assembly when the external Cu concentration is high. PccA and SenC bind Cu using Met and His residues and Cys and His residues as ligands, respectively, and both proteins form a complex during cbb3-Cox biogenesis. SenC also interacts directly with cbb3-Cox, as shown by chemical cross-linking. Here we determined the periplasmic concentrations of both proteins in vivo and analyzed their Cu binding stoichiometries and their Cu(I) and Cu(II) binding affinity constants (KD) in vitro. Our data show that both proteins bind a single Cu atom with high affinity. In vitro Cu transfer assays demonstrate Cu transfer both from PccA to SenC and from SenC to PccA at similar levels. We conclude that PccA and SenC constitute a Cu relay system that facilitates Cu delivery to cbb3-Cox.},
doi = {10.1021/acschembio.8b00293},
journal = {ACS Chemical Biology},
number = 5,
volume = 13,
place = {United States},
year = {Tue Apr 03 00:00:00 EDT 2018},
month = {Tue Apr 03 00:00:00 EDT 2018}
}

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Structural basis and mechanism for metallochaperone-assisted assembly of the CuA center in cytochrome oxidase
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