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

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.

SUBMITTER: George SJ

PROVIDER: S-EPMC5061140 | biostudies-literature | 2016 Sep

REPOSITORIES: biostudies-literature

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

George Simon J SJ Hernandez Jose A JA Jimenez-Vicente Emilio E Echavarri-Erasun Carlos C Rubio Luis M LM

Chemical communications (Cambridge, England) 20160901 79

Mo and Fe K-edge EXAFS analysis of NifQ shows the presence of a [MoFe<sub>3</sub>S<sub>4</sub>] 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. ...[more]

PMID: 27711309

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