ArticleJournal of the American Society for Mass Spectrometry2001
First observation by mass spectrometry of a 3+ oxidation state for a [4Fe-4S] metalloprotein: an ESI-FTICR mass spectrometry study of the high potential iron-sulfur protein from Chromatium vinosum.
Article in Journal of the American Society for Mass Spectrometry, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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.
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.
Who cites it
5 citing papers in PubMed, 16 citations in OpenAlex.
- Sensing mechanisms of iron-sulfur cluster regulatory proteins elucidated using native mass spectrometry.Dalton transactions (Cambridge, England : 2003) · 2021Article
- Native Mass Spectrometry of Iron-Sulfur Proteins.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Characterization of [2Fe-2S]-Cluster-Bridged Protein Complexes and Reaction Intermediates by use of Native Mass Spectrometric Methods.Angewandte Chemie (International ed. in English) · 2020Article
- Heterometallic [AgFe(3)S (4)] ferredoxin variants: synthesis, characterization, and the first crystal structure of an engineered heterometallic iron-sulfur protein.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2013Article
- Noncovalent complexes of APS reductase from M. tuberculosis: delineating a mechanistic model using ESI-FTICR MS.Journal of the American Society for Mass Spectrometry · 2007Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Electrospray ionization (ESI) Fourier transform ion cyclotron resonance mass spectrometry (FTICR) is used to measure the molecular weight of the high potential iron-sulfur protein (HiPIP) from Chromatium vinosum (C. vinosum) and its corresponding apoprotein. By accurate mass measurement of the metalloprotein, the oxidation state of the [4Fe-4S] metal center is assigned as 3+. This is the highest oxidation state yet observed by mass spectrometry for a [4Fe-4S] cluster, which usually appears in the 2+ oxidation state. In order to make this assignment correctly, the mass spectrum of the apoprotein was acquired, and a 1 Da difference was found between the molecular mass of the apoprotein and its published amino acid sequence. The mass spectra of the trypsin and cyanogen bromide digests of the alkylated apoprotein were obtained, and the data suggests that the C-terminal glycine residue is amidated.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.