Evidence map›Paper›PMID 27229513›Full record

ReviewJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2016

Mono- and binuclear non-heme iron chemistry from a theoretical perspective.

Tibor András Rokob, Jakub Chalupský, Daniel Bím, Prokopis C Andrikopoulos, Martin Srnec, Lubomír Rulíšek

Open access · greenAbstract readReview
PubMed Publisher
In one paragraph

Review in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

7 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Recent Advances in the Siderophore Biology ofFrontiers in microbiology · 2022
    Review
  4. Article
  5. Article
  6. Beyond the classical thermodynamic contributions to hydrogen atom abstraction reactivity.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  7. Article
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

6 authors at 3 institutions in 2 countries.

Tibor András RokobInstitute of Organic Chemistry, Research Centre for Natural Sciences, HAS, P.O.Box 286, Budapest, 1519, Hungary.
Jakub ChalupskýInstitute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, Gilead Sciences & IOCB Research Center, Flemingovo náměstí 2, 166 10, Prague 6, Czech Republic.
Daniel BímInstitute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, Gilead Sciences & IOCB Research Center, Flemingovo náměstí 2, 166 10, Prague 6, Czech Republic.
Prokopis C AndrikopoulosInstitute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, Gilead Sciences & IOCB Research Center, Flemingovo náměstí 2, 166 10, Prague 6, Czech Republic.
Martin SrnecJ. Heyrovský Institute of Physical Chemistry, Academy of Sciences of the Czech Republic, Dolejškova 3, 182 23, Prague 8, Czech Republic. srnec@jh-inst.cas.cz.
Lubomír RulíšekInstitute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, Gilead Sciences & IOCB Research Center, Flemingovo náměstí 2, 166 10, Prague 6, Czech Republic. rulisek@uochb.cas.cz.
Czech Academy of Sciences, Institute of Organic Chemistry and Biochemistry · CZCzech Academy of Sciences, J. Heyrovský Institute of Physical Chemistry · CZHUN-REN Research Centre for Natural Sciences · HU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In this minireview, we provide an account of the current state-of-the-art developments in the area of mono- and binuclear non-heme enzymes (NHFe and NHFe2) and the smaller NHFe(2) synthetic models, mostly from a theoretical and computational perspective. The sheer complexity, and at the same time the beauty, of the NHFe(2) world represents a challenge for experimental as well as theoretical methods. We emphasize that the concerted progress on both theoretical and experimental side is a conditio sine qua non for future understanding, exploration and utilization of the NHFe(2) systems. After briefly discussing the current challenges and advances in the computational methodology, we review the recent spectroscopic and computational studies of NHFe(2) enzymatic and inorganic systems and highlight the correlations between various experimental data (spectroscopic, kinetic, thermodynamic, electrochemical) and computations. Throughout, we attempt to keep in mind the most fascinating and attractive phenomenon in the NHFe(2) chemistry, which is the fact that despite the strong oxidative power of many reactive intermediates, the NHFe(2) enzymes perform catalysis with high selectivity. We conclude with our personal viewpoint and hope that further developments in quantum chemistry and especially in the field of multireference wave function methods are needed to have a solid theoretical basis for the NHFe(2) studies, mostly by providing benchmarking and calibration of the computationally efficient and easy-to-use DFT methods.

Indexed as

Quantum TheoryHumansNonheme Iron ProteinsNonheme Iron ProteinsDensity functional theoryDioxygen activationMultireference methodsNon-heme ironReactivity

Identifiers

PMID27229513
OpenAlexW2398174906

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.