Evidence map›Paper›PMID 16341544›Full record

ArticlePlanta2006

Nitric oxide scavenging by barley hemoglobin is facilitated by a monodehydroascorbate reductase-mediated ascorbate reduction of methemoglobin.

Abir U Igamberdiev, Natalia V Bykova, Robert D Hill

Abstract read
PubMed Publisher
In one paragraph

Article in Planta, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

36 citing papers in PubMed, 126 citations in OpenAlex.

  1. Review
  2. Review
  3. The ascorbate-glutathione cycle coming of age.Journal of experimental botany · 2024
    Review
  4. Nitric Oxide and Globin Glb1 RegulateAntioxidants (Basel, Switzerland) · 2023
    Article
  5. Review
  6. Article
  7. Flooding Tolerance in Sweet Potato (Antioxidants (Basel, Switzerland) · 2022
    Article
  8. Expressed Soybean Leghemoglobin: Effect onMolecules (Basel, Switzerland) · 2021
    Article
  9. Review
  10. Tolerant mechanisms to OJournal of plant research · 2020
    Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. 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

3 authors at 2 institutions in 1 country.

Abir U IgamberdievDepartment of Plant Science, University of Manitoba, Winnipeg, MB, R3T 2N2 Canada.
Natalia V Bykova
Robert D Hill
University of Manitoba · CAAgriculture and Agri-Food Canada · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

NADH-dependent NO scavenging in barley extracts is linked to hemoglobin (Hb) expression and is inhibited by SH-reagents. Barley Hb has a single cysteine residue. To determine whether this cysteine was critical for NO scavenging, barley Hb and a mutated version, in which the single Cys(79) was replaced by Ser, were over-expressed in Escherichia coli and purified to near homogeneity. The purified proteins exhibited very low NO-scavenging activity (12-14 nmol min(-1) mg(-1) protein) in the presence of NADH or NADPH. This activity was insensitive to SH-reagents. Addition of an extract from barley roots to either of the purified proteins resulted in high NADH-dependent NO turnover in a reaction that was sensitive to SH-reagents. A protein was purified from barley roots and identified by mass-spectrometry analysis as a cytosolic monodehydroascorbate reductase. It efficiently supported NADH-dependent NO scavenging in the presence of either native or mutated barley Hb. Ascorbate strongly facilitated the rate of metHb reduction. The K (m) for Hb was 0.3 microM, for ascorbate 0.6 mM and for NADH 4 microM. The reaction in the presence of monodehydroascorbate reductase was sensitive to SH-reagents with either form of the Hb. We conclude that metHb reduction and NO turnover do not involve direct participation of the Cys(79) residue of barley Hb. NO scavenging is facilitated by monodehydroascorbate reductase mediating a coupled reaction involving ferric Hb reduction in the presence of ascorbate and NADH.

Indexed as

Ascorbic AcidCysteineHemoglobinsHordeumMethemoglobinMutant ProteinsNADNADH, NADPH OxidoreductasesNitric OxidePlant ProteinsRecombinant ProteinsAscorbic AcidCysteineHemoglobinsMethemoglobinmonodehydroascorbate reductase (NADH)Mutant ProteinsNADNADH, NADPH OxidoreductasesNitric OxidePlant ProteinsRecombinant Proteins

Identifiers

PMID16341544
OpenAlexW2056786129

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.