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Nitrogenase and homologs

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Abstract

Nitrogenase catalyzes biological nitrogen fixation, a key step in the global nitrogen cycle. Three homologous nitrogenases have been identified to date, along with several structural and/or functional homologs of this enzyme that are involved in nitrogenase assembly, bacteriochlorophyll biosynthesis and methanogenic process, respectively. In this article, we provide an overview of the structures and functions of nitrogenase and its homologs, which highlights the similarity and disparity of this uniquely versatile group of enzymes.

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Notes

  1. The heterogeneity of earlier VFe protein preparations, which likely resulted in a mixture of different cluster species, has hampered a thorough investigation of the physiochemical properties of this protein for a long time. Taking advantage of a fast, affinity chromatography-based purification procedure, a His-tagged VFe protein was later purified from A. vinelandii as a homogeneous species with high specific activity [46]. In these homogeneous protein preparations, the P-cluster-associated S = 1/2 signal, which was previously assigned to an inactive protein species, displays a clear correlation to the specific activity of the proteins, suggesting that this P-cluster species (designated the P*-cluster) is associated with an active form of the protein. An identical S = 1/2 signal is also present in a cofactor-deplete, yet P-cluster-replete form of VFe protein, further establishing the P*-cluster as the origin of this S = 1/2 signal. Moreover, the Fe K-edge XAS/EXAFS analysis of this cofactor-deficient VFe protein suggests that the P*-cluster differs from the standard [Fe8S7] structure of the P-cluster and likely consists of paired [Fe4S4]-like clusters [5].

Abbreviations

EPR:

Electron paramagnetic resonance

ENDOR:

Electron-nuclear double resonance

ESEEM:

Electron spin echo envelope modulation

EXAFS:

Extended X-ray absorption fine structure

Fe protein:

Iron protein

FeFe protein:

Iron-iron protein

MoFe protein:

Molybdenum-iron protein

SAXS:

Small angle X-ray scattering

VFe protein:

Vanadium-iron protein

XAS:

X-ray absorption spectroscopy

XES:

X-ray emission spectroscopy

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Acknowledgments

This work was supported by National Institutes of Health grant GM 67626 (M.W.R.).

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Authors and Affiliations

  1. Department of Molecular Biology and Biochemistry, 2230 McGaugh Hall, University of California, Irvine, CA, 92697-3900, USA

    Yilin Hu

  2. Department of Molecular Biology and Biochemistry, 2236 McGaugh Hall, University of California, Irvine, CA, 92697-3900, USA

    Markus W. Ribbe

  3. Department of Chemistry, University of California, Irvine, CA, 92697-2025, USA

    Markus W. Ribbe

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Hu, Y., Ribbe, M.W. Nitrogenase and homologs. J Biol Inorg Chem 20, 435–445 (2015). https://doi.org/10.1007/s00775-014-1225-3

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