TUHH Open Research
Help
  • Log In
    New user? Click here to register.Have you forgotten your password?
  • English
  • Deutsch
  • Communities & Collections
  • Publications
  • Research Data
  • People
  • Institutions
  • Projects
  • Statistics
  1. Home
  2. TUHH
  3. Publication References
  4. Investigation of the electron transport chain to and the catalytic activity of the diheme cytochrome c peroxidase CcpA of Shewanella oneidensis
 
Options

Investigation of the electron transport chain to and the catalytic activity of the diheme cytochrome c peroxidase CcpA of Shewanella oneidensis

Publikationstyp
Journal Article
Date Issued
2011-08-24
Sprache
English
Author(s)
Schütz, Björn  
Seidel, Julian  
Sturm, Gunnar  
Einsle, Oliver  
Gescher, Johannes 
TORE-URI
http://hdl.handle.net/11420/14670
Journal
Applied and environmental microbiology  
Volume
77
Issue
17
Start Page
6172
End Page
6180
Citation
Applied and Environmental Microbiology 77 (17): 6172-6180 (2011-09-01)
Publisher DOI
10.1128/AEM.00606-11
Scopus ID
2-s2.0-80052714737
PubMed ID
21742904
Publisher
Soc.
Bacterial diheme c-type cytochrome peroxidases (BCCPs) catalyze the periplasmic reduction of hydrogen peroxide to water. The gammaproteobacterium Shewanella oneidensis produces the peroxidase CcpA under a number of anaerobic conditions, including dissimilatory iron-reducing conditions. We wanted to understand the function of this protein in the organism and its putative connection to the electron transport chain to ferric iron. CcpA was isolated and tested for peroxidase activity, and its structural conformation was analyzed by X-ray crystallography. CcpA exhibited in vitro peroxidase activity and had a structure typical of diheme peroxidases. It was produced in almost equal amounts under anaerobic and microaerophilic conditions. With 50 mM ferric citrate and 50 μM oxygen in the growth medium, CcpA expression results in a strong selective advantage for the cell, which was detected in competitive growth experiments with wild-type and ΔccpA mutant cells that lack the entire ccpA gene due to a markerless deletion. We were unable to reduce CcpA directly with CymA, MtrA, or FccA, which are known key players in the chain of electron transport to ferric iron and fumarate but identified the small monoheme ScyA as a mediator of electron transport between CymA and BCCP. To our knowledge, this is the first detailed description of a complete chain of electron transport to a periplasmic c-type cytochrome peroxidase. This study furthermore reports the possibility of establishing a specific electron transport chain using c-type cytochromes.
DDC Class
570: Biowissenschaften, Biologie
600: Technik
TUHH
Weiterführende Links
  • Contact
  • Send Feedback
  • Cookie settings
  • Privacy policy
  • Impress
DSpace Software

Built with DSpace-CRIS software - Extension maintained and optimized by 4Science
Design by effective webwork GmbH

  • Deutsche NationalbibliothekDeutsche Nationalbibliothek
  • ORCiD Member OrganizationORCiD Member Organization
  • DataCiteDataCite
  • Re3DataRe3Data
  • OpenDOAROpenDOAR
  • OpenAireOpenAire
  • BASE Bielefeld Academic Search EngineBASE Bielefeld Academic Search Engine
Feedback