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EPR spectroscopy of putative enzyme intermediates in the NO reductase and the auto-nitrosylation reaction of Desulfovibrio vulgaris hybrid cluster protein.
FEBS Lett 2019FL

Abstract

The hybrid cluster protein (Hcp) contains a unique 4Fe cluster that is a hybrid of μ-S and μ-O bridges. Escherichia coli Hcp has recently been found to carry NO reductase activity as well as S-nitrosylation activity in NO-based signaling. In other species, the physiological activity has not been established. No reaction mechanism of any Hcp has been proposed. Here, we show that Desulfovibrio vulgaris (Hildenborough) Hcp has nitric oxide reductase activity with benzyl viologen as electron donor. With EPR spectroscopy, we identify three unexpected putative reaction intermediates: both in reduced and oxidized Hcp, dinitrosyl iron complexes are formed. Also, the hybrid cluster in reduced Hcp, but not in oxidized Hcp, binds the product N2 O. Possible implications for a reaction mechanism are discussed.

Authors+Show Affiliations

Department of Biotechnology, Delft University of Technology, Delft, the Netherlands.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

31318443

Citation

Hagen, Wilfred R.. "EPR Spectroscopy of Putative Enzyme Intermediates in the NO Reductase and the Auto-nitrosylation Reaction of Desulfovibrio Vulgaris Hybrid Cluster Protein." FEBS Letters, 2019.
Hagen WR. EPR spectroscopy of putative enzyme intermediates in the NO reductase and the auto-nitrosylation reaction of Desulfovibrio vulgaris hybrid cluster protein. FEBS Lett. 2019.
Hagen, W. R. (2019). EPR spectroscopy of putative enzyme intermediates in the NO reductase and the auto-nitrosylation reaction of Desulfovibrio vulgaris hybrid cluster protein. FEBS Letters, doi:10.1002/1873-3468.13539.
Hagen WR. EPR Spectroscopy of Putative Enzyme Intermediates in the NO Reductase and the Auto-nitrosylation Reaction of Desulfovibrio Vulgaris Hybrid Cluster Protein. FEBS Lett. 2019 Jul 18; PubMed PMID: 31318443.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - EPR spectroscopy of putative enzyme intermediates in the NO reductase and the auto-nitrosylation reaction of Desulfovibrio vulgaris hybrid cluster protein. A1 - Hagen,Wilfred R, Y1 - 2019/07/18/ PY - 2019/05/11/received PY - 2019/07/10/revised PY - 2019/07/10/accepted PY - 2019/7/19/pubmed PY - 2019/7/19/medline PY - 2019/7/19/entrez KW - Desulfovibrio KW - EPR KW - NO reductase KW - hybrid cluster protein KW - nitric oxide KW - nitrosylation JF - FEBS letters JO - FEBS Lett. N2 - The hybrid cluster protein (Hcp) contains a unique 4Fe cluster that is a hybrid of μ-S and μ-O bridges. Escherichia coli Hcp has recently been found to carry NO reductase activity as well as S-nitrosylation activity in NO-based signaling. In other species, the physiological activity has not been established. No reaction mechanism of any Hcp has been proposed. Here, we show that Desulfovibrio vulgaris (Hildenborough) Hcp has nitric oxide reductase activity with benzyl viologen as electron donor. With EPR spectroscopy, we identify three unexpected putative reaction intermediates: both in reduced and oxidized Hcp, dinitrosyl iron complexes are formed. Also, the hybrid cluster in reduced Hcp, but not in oxidized Hcp, binds the product N2 O. Possible implications for a reaction mechanism are discussed. SN - 1873-3468 UR - https://www.unboundmedicine.com/medline/citation/31318443/EPR_spectroscopy_of_putative_enzyme_intermediates_in_the_NO_reductase_and_the_auto-nitrosylation_reaction_of_Desulfovibrio_vulgaris_hybrid_cluster_protein L2 - https://doi.org/10.1002/1873-3468.13539 DB - PRIME DP - Unbound Medicine ER -
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