Evidence map›Paper›PMID 16228517›Full record

ArticlePhotosynthesis research2002

Mutations of basic arginine residue 334 in the D1 protein of Photosystem II lead to unusual S(2) state properties in Synechocystis sp. PCC 6803.

Zhaoliang Li, Robert L Burnap

Abstract read
PubMed Publisher
In one paragraph

Article in Photosynthesis research, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.3field-weighted citation impact, top 44% 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

2 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. 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

2 authors at 1 institution in 1 country.

Zhaoliang LiDepartment of Microbiology and Molecular Genetics, Oklahoma State University, Stillwater, OK, 74078, USA, burnap@biochem.okstate.edu.
Robert L Burnap
Oklahoma State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The C-terminus region of the D1 protein of Photosystem II (PS II) is situated on the lumenal side of the complex and is likely to be involved in the coordination of the active site Mn atoms of the water oxidation complex (WOC). The strictly conserved arginine at position 334 (D1-334) was targeted for site-directed mutagenesis to explore the hypothesis that it is involved in the PS II extrinsic protein binding, chloride binding, or proton transfer. Although it was found that D1-R334 probably not essential for these functions, mutations at this position were found to uniquely alter the kinetics of S-state cycling in general and the properties of the S(2) state in particular. Substitutions of a glutamate (D1-R334E) and a valine (D1-R334V) for D1-R334 lead to an unusually stable (t (1/2) >30 min at room temp) S(2) state, but not S(3), as measured by double flash measurements on the bare platinum electrode. However, measurements of fluorescence decay in the presence of DCMU suggest the S(2) state is only modestly affected by the mutations. Possible reasons for these apparently contradictory results are discussed.

Identifiers

PMID16228517
OpenAlexW401490511

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.