Journal Article

PUBDB-2022-04000

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Preparation and spectroscopic characterization of lyophilized Mo nitrogenase

Van Stappen, C. (Corresponding author)Extern* ; Decamps, L.Extern* ; DeBeer, S.Extern*

2021
Springer New York

This record in other databases:        

Please use a persistent id in citations: doi:10.1007/s00775-020-01838-4  doi:10.3204/PUBDB-2022-04000

Abstract: Mo nitrogenase is the primary source of biologically fxed nitrogen, making this system highly interesting for developingnew, energy efcient ways of ammonia production. Although heavily investigated, studies of the active site of this enzymehave generally been limited to spectroscopic methods that are compatible with the presence of water and relatively low protein concentrations. One method of overcoming this limitation is through lyophilization, which allows for measurements tobe performed on solvent free, high concentration samples. This method also has the potential for allowing efcient proteinstorage and solvent exchange. To investigate the viability of this preparatory method with Mo nitrogenase, we employ acombination of electron paramagnetic resonance, Mo and Fe K-edge X-ray absorption spectroscopy, and acetylene reduction assays. Our results show that while some small distortions in the metallocofactors occur, oxidation and spin states aremaintained through the lyophilization process and that reconstitution of either lyophilized protein component into buferrestores acetylene reducing activity.

---

Contributing Institute(s):

1. DOOR-User (DOOR ; HAS-User)

Research Program(s):

1. 6G3 - PETRA III (DESY) (POF4-6G3) (POF4-6G3)

Experiment(s):

1. PETRA Beamline P64 (PETRA III)

---

Database coverage:
; ; ; BIOSIS Previews ; Biological Abstracts ; Clarivate Analytics Master Journal List ; Current Contents - Life Sciences ; Current Contents - Physical, Chemical and Earth Sciences ; DEAL Springer ; Ebsco Academic Search ; Essential Science Indicators ; IF < 5 ; JCR ; Nationallizenz ; SCOPUS ; Science Citation Index Expanded ; Web of Science Core Collection

---