English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Specificity of small c-type cytochromes in anaerobic ammonium oxidation

Akram, M., Bock, J., Dietl, A., & Barends, T. R. (2021). Specificity of small c-type cytochromes in anaerobic ammonium oxidation. ACS Omega, 6(33), 21457-21464. doi:10.1021/acsomega.1c02275.

Item is

Basic

show hide
Genre: Journal Article

Files

show Files
hide Files
:
ACSOmega_6_2021_21457.pdf (Any fulltext), 4MB
 
File Permalink:
-
Name:
ACSOmega_6_2021_21457.pdf
Description:
-
OA-Status:
Visibility:
Restricted (Max Planck Institute for Medical Research, MHMF; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-
:
ACSOmega_6_2021_21457_Suppl.pdf (Supplementary material), 2MB
 
File Permalink:
-
Name:
ACSOmega_6_2021_21457_Suppl.pdf
Description:
-
OA-Status:
Visibility:
Restricted (Max Planck Institute for Medical Research, MHMF; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show
hide
Description:
-
OA-Status:
Description:
-
OA-Status:
Description:
-
OA-Status:

Creators

show
hide
 Creators:
Akram, Mohd1, Author           
Bock, Josephine1, Author           
Dietl, Andreas1, Author           
Barends, Thomas R.M.1, Author           
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

Content

show
hide
Free keywords: Redox reactions, Bioinorganic chemistry, Peptides and proteins, Surface interactions, Imidazoles
 Abstract: Anaerobic ammonium oxidation (anammox) is a bacterial process in which ammonium and nitrite are combined into dinitrogen gas and water, yielding energy for the cell. This process relies on a series of redox reactions catalyzed by a set of enzymes, with electrons being shuttled to and from these enzymes, likely by small cytochrome c proteins. For this system to work productively, these electron carriers require a degree of specificity toward the various possible redox partners they encounter in the cell. Here, we compare two cytochrome c proteins from the anammox model organism Kuenenia stuttgartiensis. We show that they are highly homologous, are expressed at comparable levels, share the same fold, and display highly similar redox potentials, yet one of them accepts electrons from the metabolic enzyme hydroxylamine oxidase (HAO) efficiently, whereas the other does not. An analysis of the crystal structures supplemented by Monte Carlo simulations of the transient redox interactions suggests that this difference is at least partly due to the electrostatic field surrounding the proteins, illustrating one way in which the electron carriers in anammox could attain the required specificity. Moreover, the simulations suggest a different “outlet” for electrons on HAO than has traditionally been assumed.

Details

show
hide
Language(s): eng - English
 Dates: 2021-04-302021-08-022021-08-092021-08-24
 Publication Status: Published in print
 Pages: 8
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: ACS Omega
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Washington, DC : American Chemical Society
Pages: - Volume / Issue: 6 (33) Sequence Number: - Start / End Page: 21457 - 21464 Identifier: ISSN: 2470-1343
CoNE: https://pure.mpg.de/cone/journals/resource/2470-1343