Evidence map›Paper›PMID 17554172›Full record

ArticleActa crystallographica. Section F, Structural biology and crystallization communications2007

Crystallization and preliminary X-ray diffraction studies of the ferredoxin reductase component in the Rieske nonhaem iron oxygenase system carbazole 1,9a-dioxygenase.

Yuji Ashikawa, Hiromasa Uchimura, Zui Fujimoto, Kengo Inoue, Haruko Noguchi, Hisakazu Yamane, Hideaki Nojiri

Abstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

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7citing papers in PubMed
–field-weighted citation impact
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3 · Its place in the literature

Who cites it

7 citing papers in PubMed.

  1. Article
  2. Engineering Rieske oxygenase activity one piece at a time.Current opinion in chemical biology · 2023
    Review
  3. Article
  4. Article
  5. Article
  6. Crystallization and preliminary X-ray diffraction studies of a terminal oxygenase of carbazole 1,9a-dioxygenase from Novosphingobium sp. KA1.Acta crystallographica. Section F, Structural biology and crystallization communications · 2010
    Article
  7. Article
4 · The record

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5 · Who and what money

Authors and funding

7 authors.

Yuji AshikawaBiotechnology Research Center, The University of Tokyo, Yayoi, Bunkyo-ku, Tokyo, Japan.
Hiromasa Uchimura
Zui Fujimoto
Kengo Inoue
Haruko Noguchi
Hisakazu Yamane
Hideaki Nojiri

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Carbazole 1,9a-dioxygenase (CARDO), which consists of an oxygenase component (CARDO-O) and the electron-transport components ferredoxin (CARDO-F) and ferredoxin reductase (CARDO-R), catalyzes dihydroxylation at the C1 and C9a positions of carbazole. CARDO-R was crystallized at 277 K using the hanging-drop vapour-diffusion method with the precipitant PEG 8000. Two crystal types (types I and II) were obtained. The type I crystal diffracted to a maximum resolution of 2.80 A and belonged to space group P4(2)2(1)2, with unit-cell parameters a = b = 158.7, c = 81.4 A. The type II crystal was obtained in drops from which type I crystals had been removed; it diffracted to 2.60 A resolution and belonged to the same space group, with unit-cell parameters a = b = 161.8, c = 79.5 A.

Indexed as

Bacterial ProteinsCrystallizationDioxygenasesElectron Transport Complex IIIFerredoxin-NADP ReductaseIron-Sulfur ProteinsNonheme Iron ProteinsX-Ray DiffractionBacterial Proteinscarbazole 1,9a-dioxygenaseDioxygenasesElectron Transport Complex IIIFerredoxin-NADP ReductaseIron-Sulfur ProteinsNonheme Iron ProteinsRieske iron-sulfur protein

Identifiers

PMID17554172
PMCPMC2335075

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.