Evidence map›Paper›PMID 40053255›Full record

ArticleFish physiology and biochemistry2025

Biochemical properties of molybdenum cofactor isolated from fish liver.

Mereke Satkanov, Zhadyrassyn Nurbekova, Alikhan Bilyalov, Diana Tazhibay, Masalimov Zhaksylyk, Maral Kulatayeva, Zhaoqi Wang, Junfang Cui, Zerekbay Alikulov

Abstract read
PubMed Publisher
In one paragraph

Article in Fish physiology and biochemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. Review
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

9 authors.

Mereke SatkanovDepartment of Biotechnology and Microbiology, L.N. Gumilyov, Eurasian National University, Astana, 010000, Kazakhstan.
Zhadyrassyn NurbekovaDepartment of Biotechnology and Microbiology, L.N. Gumilyov, Eurasian National University, Astana, 010000, Kazakhstan.
Alikhan BilyalovDepartment of Biotechnology and Microbiology, L.N. Gumilyov, Eurasian National University, Astana, 010000, Kazakhstan.
Diana TazhibayDepartment of Biotechnology and Microbiology, L.N. Gumilyov, Eurasian National University, Astana, 010000, Kazakhstan.
Masalimov ZhaksylykDepartment of Biotechnology and Microbiology, L.N. Gumilyov, Eurasian National University, Astana, 010000, Kazakhstan.
Maral KulatayevaDepartment of Biotechnology and Microbiology, L.N. Gumilyov, Eurasian National University, Astana, 010000, Kazakhstan.
Zhaoqi WangCAS Key Laboratory of Environmental and Applied Microbiology, Environmental Microbiology Key Laboratory of Sichuan Province, Chengdu Institute of Biology Chinese Academy of Sciences, Chengdu, 610041, China.
Junfang CuiInstitute of Mountain Hazards and Environment, Chinese Academy of Sciences, Chengdu, 610299, China.
Zerekbay AlikulovDepartment of Biotechnology and Microbiology, L.N. Gumilyov, Eurasian National University, Astana, 010000, Kazakhstan. zer-kaz@mail.ru.

Funding

Science Committee of the Ministry of Science and Higher Education of the Republic of Kazakhstan AP19680579
6 · The paper itself

Abstract

Recent studies have demonstrated that the fish liver protein fraction extract obtained by gel filtration exhibits nitric oxide synthase (NOS)-independent NO synthase from nitrates and nitrites. This activity was attributed to the molybdenum enzymes (Mo-enzymes) group which was already demonstrated in mammals. However, the evidence that NOS-independent NO synthase activity can be classified as a fish Mo-enzyme has been poorly demonstrated. In mammals, Mo-enzymes NOS-independent NO synthase activity occurs at the molybdenum center. We studied the ability of molybdenum cofactor (Mo-co) isolated from the protein fraction of fish liver extract to restore the NADPH-nitrate reductase (NADPH-NR) activity from Neurospora crassa nit-1. Our results demonstrated that Mo-co from the extract from fish liver was able to recover NADPH-NR activity in the extract of N. crassa nit-1, thereby possessing the ability to reduce nitrogen compounds. However, the oxidation of Mo-co from fish liver destabilizes molybdenum, leading to its inactivation. However, the results obtained under anaerobic conditions with dithionite indicate that Mo remains bound to Mo-co under highly reducing conditions. This may also indicate that the availability of Mo is not the sole factor affecting the activity of Mo-enzymes, also oxygen content after the synthesis of mature Mo-co may play a role in cofactor inactivation.

Indexed as

CoenzymesLiverMetalloproteinsMolybdenumPteridinesAnimalsMolybdenum CofactorsNitrate ReductaseOxidation-ReductionCoenzymesMetalloproteinsMolybdenumMolybdenum CofactorsmolybdopterinNitrate ReductasePteridinesFish molybdenum enzymesGel filtrationMolybdenum cofactorNeurospora crassa nit-1

Identifiers

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.