Evidence map›Paper›PMID 33441566›Full record

ArticleScientific reports2021

Color-tuning of natural variants of heliorhodopsin.

Se-Hwan Kim, Kimleng Chuon, Shin-Gyu Cho, Ahreum Choi, Seanghun Meas, Hyun-Suk Cho, Kwang-Hwan Jung

Abstract read
In one paragraph

Article in Scientific reports, 2021. 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
–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

7 citing papers in PubMed.

  1. Article
  2. Molecular properties of a viral heliorhodopsin, V2HeR2.Biophysics and physicobiology · 2025
    Article
  3. Review
  4. Article
  5. Fluorescence of the Retinal Chromophore in Microbial and Animal Rhodopsins.International journal of molecular sciences · 2023
    Review
  6. Article
  7. Evolution of the Automatic Rhodopsin Modeling (ARM) Protocol.Topics in current chemistry (Cham) · 2022
    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

7 authors.

Se-Hwan KimDepartment of Life Science and Institute of Biological Interfaces, Sogang University, 35 Baekbeom-Ro, Mapo-Gu, Seoul, 04107, Korea.
Kimleng ChuonDepartment of Life Science and Institute of Biological Interfaces, Sogang University, 35 Baekbeom-Ro, Mapo-Gu, Seoul, 04107, Korea.
Shin-Gyu ChoDepartment of Life Science and Institute of Biological Interfaces, Sogang University, 35 Baekbeom-Ro, Mapo-Gu, Seoul, 04107, Korea.
Ahreum ChoiResearch Center for Endangered Species, National Institute of Ecology, 23, Gowol-gil, Yeongyang-eup, Yeongyang-gun, 36531, Gyeongsangbuk-do, Korea.
Seanghun MeasDepartment of Life Science and Institute of Biological Interfaces, Sogang University, 35 Baekbeom-Ro, Mapo-Gu, Seoul, 04107, Korea.
Hyun-Suk ChoDepartment of Life Science and Institute of Biological Interfaces, Sogang University, 35 Baekbeom-Ro, Mapo-Gu, Seoul, 04107, Korea.
Kwang-Hwan JungDepartment of Life Science and Institute of Biological Interfaces, Sogang University, 35 Baekbeom-Ro, Mapo-Gu, Seoul, 04107, Korea. kjung@sogang.ac.kr.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Microbial rhodopsins are distributed through many microorganisms. Heliorhodopsins are newly discovered but have an unclear function. They have seven transmembrane helices similar to type-I and type-II rhodopsins, but they are different in that the N-terminal region of heliorhodopsin is cytoplasmic. We chose 13 representative heliorhodopsins from various microorganisms, expressed and purified with an N-terminal His tag, and measured the absorption spectra. The 13 natural variants had an absorption maximum (λmax) in the range 530-556 nm similar to proteorhodopsin (λmax = 490-525 nm). We selected several candidate residues that influence rhodopsin color-tuning based on sequence alignment and constructed mutants via site-directed mutagenesis to confirm the spectral changes. We found two important residues located near retinal chromophore that influence λmax. We also predict the 3D structure via homology-modeling of Thermoplasmatales heliorhodopsin. The results indicate that the color-tuning mechanism of type-I rhodopsin can be applied to understand the color-tuning of heliorhodopsin.

Identifiers

PMID33441566
PMCPMC7807009

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