Evidence map›Paper›PMID 26392147›Full record

ReviewBiochimica et biophysica acta2016

Ru(II)-diimine functionalized metalloproteins: From electron transfer studies to light-driven biocatalysis.

Quan Lam, Mallory Kato, Lionel Cheruzel

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

15 citing papers in PubMed, 38 citations in OpenAlex.

  1. Review
  2. Review
  3. Light-driven biocatalytic oxidation.Chemical science · 2022
    Review
  4. Article
  5. Advances in photosensitizer-related design for photodynamic therapy.Asian journal of pharmaceutical sciences · 2021
    Review
  6. Review
  7. Article
  8. Review
  9. Coupling efficiency in light-driven hybrid P450BM3 and CYP119 enzymes.Archives of biochemistry and biophysics · 2019
    Article
  10. Article
  11. Keeping the spotlight on cytochrome P450.Biochimica et biophysica acta. Proteins and proteomics · 2018
    Review
  12. Article
  13. Article
  14. Article
  15. 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

3 authors at 1 institution in 1 country.

Quan LamSan José State University, Department of Chemistry, One Washington Square, San José, CA 95192-0101, United States.
Mallory KatoSan José State University, Department of Chemistry, One Washington Square, San José, CA 95192-0101, United States.
Lionel CheruzelSan José State University, Department of Chemistry, One Washington Square, San José, CA 95192-0101, United States. Electronic address: lionel.cheruzel@sjsu.edu.
San Jose State University · US

Funding

Ru(II)-diimine labeled P450 mutants for the selective hydroxylation of substrateSC3GM095415 · NIGMS · SAN JOSE STATE UNIVERSITY · PI CHERUZEL, LIONEL E. · 2011 to 2018
$860k
NIGMS NIH HHS SC3 GM095415
6 · The paper itself

Abstract

The unique photochemical properties of Ru(II)-diimine complexes have helped initiate a series of seminal electron transfer studies in metalloenzymes. It has thus been possible to experimentally determine rate constants for long-range electron transfers. These studies have laid the foundation for the investigation of reactive intermediates in heme proteins and for the design of light-activated biocatalysts. Various metalloenzymes such as hydrogenase, carbon monoxide dehydrogenase, nitrogenase, laccase and cytochrome P450 BM3 have been functionalized with Ru(II)-diimine complexes. Upon visible light-excitation, these photosensitized metalloproteins are capable of sustaining photocatalytic activity to reduce small molecules such as protons, acetylene, hydrogen cyanide and carbon monoxide or activate molecular dioxygen to produce hydroxylated products. The Ru(II)-diimine photosensitizers are hence able to deliver multiple electrons to metalloenzymes buried active sites, circumventing the need for the natural redox partners. In this review, we will highlight the key achievements of the light-driven biocatalysts, which stem from the extensive electron transfer investigations. This article is part of a Special Issue entitled Biodesign for Bioenergetics--the design and engineering of electronic transfer cofactors, proteins and protein networks, edited by Ronald L. Koder and J.L. Ross Anderson.

Indexed as

Electron TransportEnergy MetabolismAnimalsCatalysisHumansIminesMetalloproteinsModels, MolecularOxidation-ReductionProtein BindingProtein EngineeringRutheniumIminesMetalloproteinsRutheniumElectron transfer studiesLight-driven biocatalysisRuthenium photosensitizers

Identifiers

PMID26392147
PMCPMC4808502
OpenAlexW2156230488

What OpenQuestion holds

Textmetadata
LicenceTDM
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.