Literature DB >> 12829270

Nickel uptake and utilization by microorganisms.

Scott B Mulrooney1, Robert P Hausinger.   

Abstract

Nickel is an essential nutrient for selected microorganisms where it participates in a variety of cellular processes. Many microbes are capable of sensing cellular nickel ion concentrations and taking up this nutrient via nickel-specific permeases or ATP-binding cassette-type transport systems. The metal ion is specifically incorporated into nickel-dependent enzymes, often via complex assembly processes requiring accessory proteins and additional non-protein components, in some cases accompanied by nucleotide triphosphate hydrolysis. To date, nine nickel-containing enzymes are known: urease, NiFe-hydrogenase, carbon monoxide dehydrogenase, acetyl-CoA decarbonylase/synthase, methyl coenzyme M reductase, certain superoxide dismutases, some glyoxylases, aci-reductone dioxygenase, and methylenediurease. Seven of these enzymes have been structurally characterized, revealing distinct metallocenter environments in each case.

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Year:  2003        PMID: 12829270     DOI: 10.1016/S0168-6445(03)00042-1

Source DB:  PubMed          Journal:  FEMS Microbiol Rev        ISSN: 0168-6445            Impact factor:   16.408


  109 in total

1.  Selenium is involved in regulation of periplasmic hydrogenase gene expression in Desulfovibrio vulgaris Hildenborough.

Authors:  Filipa M A Valente; Cláudia C Almeida; Isabel Pacheco; João Carita; Lígia M Saraiva; Inês A C Pereira
Journal:  J Bacteriol       Date:  2006-05       Impact factor: 3.490

2.  Metabolic versatility of prokaryotes for urea decomposition.

Authors:  Robert P Hausinger
Journal:  J Bacteriol       Date:  2004-05       Impact factor: 3.490

3.  Geobacter uraniireducens NikR displays a DNA binding mode distinct from other members of the NikR family.

Authors:  Erin L Benanti; Peter T Chivers
Journal:  J Bacteriol       Date:  2010-06-25       Impact factor: 3.490

4.  An ABC transporter and a TonB ortholog contribute to Helicobacter mustelae nickel and cobalt acquisition.

Authors:  Jeroen Stoof; Ernst J Kuipers; Gerard Klaver; Arnoud H M van Vliet
Journal:  Infect Immun       Date:  2010-07-19       Impact factor: 3.441

5.  Biochemical and structural studies on native and recombinant Glycine max UreG: a detailed characterization of a plant urease accessory protein.

Authors:  Rafael Real-Guerra; Fernanda Staniscuaski; Barbara Zambelli; Francesco Musiani; Stefano Ciurli; Célia R Carlini
Journal:  Plant Mol Biol       Date:  2012-01-22       Impact factor: 4.076

6.  Structural and functional role of nickel ions in urease by molecular dynamics simulation.

Authors:  Jing Lv; Yongjun Jiang; Qingsen Yu; Shaoyong Lu
Journal:  J Biol Inorg Chem       Date:  2010-10-02       Impact factor: 3.358

7.  NikR-operator complex structure and the mechanism of repressor activation by metal ions.

Authors:  Eric R Schreiter; Sheila C Wang; Deborah B Zamble; Catherine L Drennan
Journal:  Proc Natl Acad Sci U S A       Date:  2006-08-31       Impact factor: 11.205

8.  Purification and properties of the Klebsiella aerogenes UreE metal-binding domain, a functional metallochaperone of urease.

Authors:  Scott B Mulrooney; Sarah K Ward; Robert P Hausinger
Journal:  J Bacteriol       Date:  2005-05       Impact factor: 3.490

9.  Comparative and functional genomic analysis of prokaryotic nickel and cobalt uptake transporters: evidence for a novel group of ATP-binding cassette transporters.

Authors:  Dmitry A Rodionov; Peter Hebbeln; Mikhail S Gelfand; Thomas Eitinger
Journal:  J Bacteriol       Date:  2006-01       Impact factor: 3.490

10.  Binding of Ni2+ to a histidine- and glutamine-rich protein, Hpn-like.

Authors:  Yi-Bo Zeng; Dong-Mei Zhang; Hongyan Li; Hongzhe Sun
Journal:  J Biol Inorg Chem       Date:  2008-06-19       Impact factor: 3.358

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