skip to main content
US FlagAn official website of the United States government
dot gov icon
Official websites use .gov
A .gov website belongs to an official government organization in the United States.
https lock icon
Secure .gov websites use HTTPS
A lock ( lock ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

Explore Research Products in the PAR
It may take a few hours for recently added research products to appear in PAR search results.


  • Home
  • Search Results
  • Page 1 of 1

Search for: All records

Creators/Authors contains: "Jasniewski, Andrew"

Note: When clicking on a Digital Object Identifier (DOI) number, you will be taken to an external site maintained by the publisher. Some full text articles may not yet be available without a charge during the embargo (administrative interval).
What is a DOI Number?

Some links on this page may take you to non-federal websites. Their policies may differ from this site.

  1. ; ; ; ; ; ; ; ; ; (, Chemical reviews)
  2. ; ; ; ; ; ; ; ; ; ; et al (, ChemBioChem)
    Accepted Manuscript Full Text Available
  3. ; ; ; (, Chemical Reviews)
    Full Text Available 
  4. ; ; ; (, Inorganics)
    Full Text Available 
  5. ; ; ; ; ; ; ; ; ; (, Inorganic Chemistry)
    Full Text Available 
  6. ; ; ; ; ; ; ; (, Angewandte Chemie International Edition)
    Abstract The Fe protein of nitrogenase plays multiple roles in substrate reduction and cluster maturation via its redox‐active [Fe4S4] cluster. Here we report the synthesis and characterization of a water‐soluble [Fe4Se4] cluster that is used to substitute the [Fe4S4] cluster of theAzotobacter vinelandiiFe protein (AvNifH). Biochemical, EPR and XAS/EXAFS analyses demonstrate the ability of the [Fe4Se4] cluster to adopt the super‐reduced, all‐ferrous state upon its incorporation intoAvNifH. Moreover, these studies reveal that the [Fe4Se4] cluster inAvNifH already assumes a partial all‐ferrous state ([Fe4Se4]0) in the presence of dithionite, where its [Fe4S4] counterpart inAvNifH exists solely in the reduced state ([Fe4S4]1+). Such a discrepancy in the redox properties of theAvNifH‐associated [Fe4Se4] and [Fe4S4] clusters can be used to distinguish the differential redox requirements for the substrate reduction and cluster maturation of nitrogenase, pointing to the utility of chalcogen‐substituted FeS clusters in future mechanistic studies of nitrogenase catalysis and assembly. 
    more » « less