Issue 79, 2016
From the journal:

Chemical Communications

EXAFS reveals two Mo environments in the nitrogenase iron–molybdenum cofactor biosynthetic protein NifQ†

Simon J. George,‡a   Jose A. Hernandez,‡b   Emilio Jimenez-Vicente,c   Carlos Echavarri-Erasunc  and  Luis M. Rubio*c  

* Corresponding authors

a Simon Scientific Inc., Berkeley, California, USA

b Department of Biochemistry, Midwestern University, Glendale, Arizona, USA

c Centro de Biotecnología y Genómica de Plantas, Universidad Politénica de Madrid (UPM), Instituto Nacional de Investigación y Tecnología Agraria y Alimentaria (INIA), Campus Montegancedo UPM, Pozuelo de Alarcón, Madrid, Spain
E-mail: lm.rubio@upm.es

Abstract

Mo and Fe K-edge EXAFS analysis of NifQ shows the presence of a [MoFe3S4] cluster and a second independent Mo environment that includes Mo–O bonds and Mo–S bonds. Both environments are relevant to FeMo-co biosynthesis and may represent different stages of Mo biochemical transformations catalyzed by NifQ.

Graphical abstract: EXAFS reveals two Mo environments in the nitrogenase iron–molybdenum cofactor biosynthetic protein NifQ

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Article information

DOI
https://doi.org/10.1039/C6CC06370E
Article type
Communication
Submitted
02 Aug 2016
Accepted
09 Sep 2016
First published
09 Sep 2016

Chem. Commun., 2016,52, 11811-11814

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EXAFS reveals two Mo environments in the nitrogenase iron–molybdenum cofactor biosynthetic protein NifQ

S. J. George, J. A. Hernandez, E. Jimenez-Vicente, C. Echavarri-Erasun and L. M. Rubio, Chem. Commun., 2016, 52, 11811 DOI: 10.1039/C6CC06370E

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