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No formation by a catalytically self-sufficient bacterial nitric oxide synthase from sorangium cellulosum

Academic Article
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Overview

authors

  • Agapie, T.
  • Suseno, S.
  • Woodward, J. J.
  • Stoll, S.
  • Britt, R. D.
  • Marletta, Michael

publication date

  • September 2009

journal

  • Proceedings of the National Academy of Sciences of the United States of America  Journal

abstract

  • The role of nitric oxide (NO) in the host response to infection and in cellular signaling is well established. Enzymatic synthesis of NO is catalyzed by the nitric oxide synthases (NOSs), which convert Arg into NO and citrulline using co-substrates O2 and NADPH. Mammalian NOS contains a flavin reductase domain (FAD and FMN) and a catalytic heme oxygenase domain (P450-type heme and tetrahydrobiopterin). Bacterial NOSs, while much less studied, were previously identified as only containing the heme oxygenase domain of the more complex mammalian NOSs. We report here on the characterization of a NOS from Sorangium cellulosum (both full-length, scNOS, and oxygenase domain, scNOSox). scNOS contains a catalytic, oxygenase domain similar to those found in the mammalian NOS and in other bacteria. Unlike the other bacterial NOSs reported to date, however, this protein contains a fused reductase domain. The scNOS reductase domain is unique for the entire NOS family because it utilizes a 2Fe2S cluster for electron transfer. scNOS catalytically produces NO and citrulline in the presence of either tetrahydrobiopterin or tetrahydrofolate. These results establish a bacterial electron transfer pathway used for biological NO synthesis as well as a unique flexibility in using different tetrahydropterin cofactors for this reaction.

subject areas

  • Amino Acid Sequence
  • Bacterial Proteins
  • Binding Sites
  • Catalysis
  • Electron Spin Resonance Spectroscopy
  • Electron Transport
  • Electrophoresis, Polyacrylamide Gel
  • Heme
  • Kinetics
  • Models, Chemical
  • Molecular Sequence Data
  • Myxococcales
  • NADP
  • Nitric Oxide
  • Nitric Oxide Synthase
  • Oxidation-Reduction
  • Oxygen
  • Protein Binding
  • Sequence Homology, Amino Acid
  • Spectrophotometry, Ultraviolet
  • Substrate Specificity
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Research

keywords

  • heme protein
  • iron-sulfur cluster
  • reductase
  • tetrahydrobiopterin
  • tetrahydrofolate
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Identity

PubMed Central ID

  • PMC2752531

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.0908443106

PubMed ID

  • 19805284
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Additional Document Info

start page

  • 16221

end page

  • 16226

volume

  • 106

issue

  • 38

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