Evidence map›Paper›PMID 26092463›Full record

ArticleApplied and environmental microbiology2015

New Insight into Microbial Iron Oxidation as Revealed by the Proteomic Profile of an Obligate Iron-Oxidizing Chemolithoautotroph.

Roman A Barco, David Emerson, Jason B Sylvan, Beth N Orcutt, Myrna E Jacobson Meyers, Gustavo A Ramírez, John D Zhong, Katrina J Edwards

Open access · bronzeAbstract read
In one paragraph

Article in Applied and environmental microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.

0numbers the graph read from it
0cells of the map it votes in
74citing papers in PubMed
10.7field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

74 citing papers in PubMed, 145 citations in OpenAlex.

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  18. Heterotrophic Sulfur Oxidation ofFrontiers in microbiology · 2022
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  20. Oligo-heterotrophic Activity ofApplied and environmental microbiology · 2021
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14 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 1 country.

Roman A BarcoDepartment of Biological Sciences, University of Southern California, Los Angeles, California, USA barco@usc.edu.
David EmersonBigelow Laboratory for Ocean Sciences, East Boothbay, Maine, USA.
Jason B SylvanDepartment of Biological Sciences, University of Southern California, Los Angeles, California, USA.
Beth N OrcuttBigelow Laboratory for Ocean Sciences, East Boothbay, Maine, USA.
Myrna E Jacobson MeyersDepartment of Biological Sciences, University of Southern California, Los Angeles, California, USA.
Gustavo A RamírezDepartment of Biological Sciences, University of Southern California, Los Angeles, California, USA.
John D ZhongDepartment of Biological Sciences, University of Southern California, Los Angeles, California, USA.
Katrina J EdwardsDepartment of Biological Sciences, University of Southern California, Los Angeles, California, USA.
University of Southern California · USBigelow Laboratory for Ocean Sciences · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Microaerophilic, neutrophilic, iron-oxidizing bacteria (FeOB) grow via the oxidation of reduced Fe(II) at or near neutral pH, in the presence of oxygen, making them relevant in numerous environments with elevated Fe(II) concentrations. However, the biochemical mechanisms for Fe(II) oxidation by these neutrophilic FeOB are unknown, and genetic markers for this process are unavailable. In the ocean, microaerophilic microorganisms in the genus Mariprofundus of the class Zetaproteobacteria are the only organisms known to chemolithoautotrophically oxidize Fe and concurrently biomineralize it in the form of twisted stalks of iron oxyhydroxides. The aim of this study was to identify highly expressed proteins associated with the electron transport chain of microaerophilic, neutrophilic FeOB. To this end, Mariprofundus ferrooxydans PV-1 was cultivated, and its proteins were extracted, assayed for redox activity, and analyzed via liquid chromatography-tandem mass spectrometry for identification of peptides. The results indicate that a cytochrome c4, cbb3-type cytochrome oxidase subunits, and an outer membrane cytochrome c were among the most highly expressed proteins and suggest an involvement in the process of aerobic, neutrophilic bacterial Fe oxidation. Proteins associated with alternative complex III, phosphate transport, carbon fixation, and biofilm formation were abundant, consistent with the lifestyle of Mariprofundus.

Indexed as

Bacterial ProteinsChemoautotrophic GrowthIronMolecular Sequence DataOxidation-ReductionProteobacteriaProteomicsBacterial ProteinsIron

Identifiers

PMID26092463
PMCPMC4551237
OpenAlexW2149194791

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.