Literature DB >> 3680176

A Pseudomonas stutzeri outer membrane protein inserts copper into N2O reductase.

K Mokhele1, Y J Tang, M A Clark, J L Ingraham.   

Abstract

Among a set of frameshift mutagen (ICR-191; Polysciences, Inc.)-induced mutations that confer inability to grow anaerobically with N2O as the sole electron acceptor, one class was found that produced an inactive N2O reductase which lacked copper. All of these mutant strains failed to produce a 61,000-Mr protein located in the outer membrane. This protein, termed NosA, seems not to be responsible for bringing copper into the cell because the mutant strains and their parent were similarly sensitive to the copper content of the growth medium and no intermediate copper concentration in the medium permitted the mutant strains (nosA) to grow anaerobically with N2O as the sole electron acceptor. We conclude that NosA is necessary to insert copper into N2O reductase or to maintain it there.

Entities:  

Mesh:

Substances:

Year:  1987        PMID: 3680176      PMCID: PMC214080          DOI: 10.1128/jb.169.12.5721-5726.1987

Source DB:  PubMed          Journal:  J Bacteriol        ISSN: 0021-9193            Impact factor:   3.490


  14 in total

1.  Outer membranes of gram-negative bacteria. XIX. Isolation from Pseudomonas aeruginosa PAO1 and use in reconstitution and definition of the permeability barrier.

Authors:  R E Hancock; H Nikaido
Journal:  J Bacteriol       Date:  1978-10       Impact factor: 3.490

2.  STUDIES ON THE GRAM-NEGATIVE CELL WALL. I. EVIDENCE FOR THE ROLE OF 2-KETO- 3-DEOXYOCTONATE IN THE LIPOPOLYSACCHARIDE OF SALMONELLA TYPHIMURIUM.

Authors:  M J OSBORN
Journal:  Proc Natl Acad Sci U S A       Date:  1963-09       Impact factor: 11.205

3.  High resolution two-dimensional electrophoresis of proteins.

Authors:  P H O'Farrell
Journal:  J Biol Chem       Date:  1975-05-25       Impact factor: 5.157

4.  A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding.

Authors:  M M Bradford
Journal:  Anal Biochem       Date:  1976-05-07       Impact factor: 3.365

5.  Cleavage of structural proteins during the assembly of the head of bacteriophage T4.

Authors:  U K Laemmli
Journal:  Nature       Date:  1970-08-15       Impact factor: 49.962

6.  Evidence for an active role of donor cells in natural transformation of Pseudomonas stutzeri.

Authors:  G J Stewart; C A Carlson; J L Ingraham
Journal:  J Bacteriol       Date:  1983-10       Impact factor: 3.490

7.  Separation of the cytoplasmic and outer membrane of Pseudomonas aeruginosa PAQ.

Authors:  B R Booth; N A Curtis
Journal:  Biochem Biophys Res Commun       Date:  1977-02-07       Impact factor: 3.575

8.  First practical assay for soluble nitrous oxide reductase of denitrifying bacteria and a partial kinetic characterization.

Authors:  J K Kristjansson; T C Hollocher
Journal:  J Biol Chem       Date:  1980-01-25       Impact factor: 5.157

9.  Pseudomonas stutzeri and related species undergo natural transformation.

Authors:  C A Carlson; L S Pierson; J J Rosen; J L Ingraham
Journal:  J Bacteriol       Date:  1983-01       Impact factor: 3.490

10.  Isolation and characterization of transposon Tn5-induced mutants of Pseudomonas perfectomarina defective in nitrous oxide respiration.

Authors:  W G Zumft; K Döhler; H Körner
Journal:  J Bacteriol       Date:  1985-09       Impact factor: 3.490

View more
  11 in total

1.  Periplasmic location of nitrous oxide reductase and its apoform in denitrifying Pseudomonas stutzeri.

Authors:  H Körner; F Mayer
Journal:  Arch Microbiol       Date:  1992       Impact factor: 2.552

Review 2.  Metabolic pathways in Paracoccus denitrificans and closely related bacteria in relation to the phylogeny of prokaryotes.

Authors:  A H Stouthamer
Journal:  Antonie Van Leeuwenhoek       Date:  1992-01       Impact factor: 2.271

Review 3.  Metabolic regulation including anaerobic metabolism in Paracoccus denitrificans.

Authors:  A H Stouthamer
Journal:  J Bioenerg Biomembr       Date:  1991-04       Impact factor: 2.945

4.  Properties of a Pseudomonas stutzeri outer membrane channel-forming protein (NosA) required for production of copper-containing N2O reductase.

Authors:  H S Lee; R E Hancock; J L Ingraham
Journal:  J Bacteriol       Date:  1989-04       Impact factor: 3.490

5.  Molecular cloning, heterologous expression, and primary structure of the structural gene for the copper enzyme nitrous oxide reductase from denitrifying Pseudomonas stutzeri.

Authors:  A Viebrock; W G Zumft
Journal:  J Bacteriol       Date:  1988-10       Impact factor: 3.490

Review 6.  Cell biology and molecular basis of denitrification.

Authors:  W G Zumft
Journal:  Microbiol Mol Biol Rev       Date:  1997-12       Impact factor: 11.056

7.  Dual pathways for copper uptake by methanotrophic bacteria.

Authors:  Ramakrishnan Balasubramanian; Grace E Kenney; Amy C Rosenzweig
Journal:  J Biol Chem       Date:  2011-09-07       Impact factor: 5.157

8.  Pseudomonas stutzeri N2O reductase contains CuA-type sites.

Authors:  R A Scott; W G Zumft; C L Coyle; D M Dooley
Journal:  Proc Natl Acad Sci U S A       Date:  1989-06       Impact factor: 11.205

9.  Requirements for Cu(A) and Cu-S center assembly of nitrous oxide reductase deduced from complete periplasmic enzyme maturation in the nondenitrifier Pseudomonas putida.

Authors:  Patrick Wunsch; Margitta Herb; Hagen Wieland; Ulrike M Schiek; Walter G Zumft
Journal:  J Bacteriol       Date:  2003-02       Impact factor: 3.490

10.  Molecular characterization of nosA, a Pseudomonas stutzeri gene encoding an outer membrane protein required to make copper-containing N2O reductase.

Authors:  H S Lee; A H Abdelal; M A Clark; J L Ingraham
Journal:  J Bacteriol       Date:  1991-09       Impact factor: 3.490

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.