Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2020 Jan 22;10:953. doi: 10.1038/s41598-020-57587-6

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© The Author(s) 2020

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

PMC Copyright notice

The atypical heme binding site of SirA is required for maturation and stability. (a) Locations of typical and atypical heme binding sites of SirA. Black boxes indicate typical CXXCH binding sites, the gray box indicates the atypical CX₁₂NKGCH binding site. Asparagine 589 (bolded) was changed to a cystine to restore the atypical binding site to the typical CXXCH motif. (b) Shewanella that expressed the wildtype or mutated SirA were grown anaerobically on sulfite. The SirA_N589C mutant was unable to reduce sulfite, as indicated by lack of hydrogen sulfide production. (c) Whole cell extracts from the wildtype, ΔsirA and SirA_N589C strains were tested for sulfite reductase activity and the SirA protein. Neither ΔsirA nor SirA_N589C cell extracts had an active sulfite reductase or a band that reacted with antibodies directed against SirA. Full-length blots/gels are presented in Supplementary Fig. S3.