Evidence map›Paper›PMID 33475096›Full record

ReviewChemical Society reviews2021

Molecular understanding of heteronuclear active sites in heme-copper oxidases, nitric oxide reductases, and sulfite reductases through biomimetic modelling.

Christopher J Reed, Quan N Lam, Evan N Mirts, Yi Lu

Open access · greenAbstract readReview
In one paragraph

Review in Chemical Society reviews, 2021. 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
3.4field-weighted citation impact, top 7% 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, 53 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. A Bioinspired Nonheme FeJournal of the American Chemical Society · 2024
    Article
  9. Heme-copper and Heme OJournal of inorganic biochemistry · 2023
    Review
  10. Article
  11. Review
  12. Review
  13. Protein Assembly by Design.Chemical reviews · 2021
    Review
  14. Review
  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

4 authors at 1 institution in 2 countries.

Christopher J ReedDepartment of Chemistry, University of Illinois at Urbana-Champaign, Urban, IL 61801, USA. yi-lu@illinois.edu.ORCID http://orcid.org/0000-0002-8774-5106
Quan N LamDepartment of Biochemistry, University of Illinois at Urbana-Champaign, Urban, IL 61801, USA.
Evan N MirtsCenter for Biophysics and Quantitative Biology, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA and Carl R. Woese Institute for Genomic Biology, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.
Yi LuDepartment of Chemistry, University of Illinois at Urbana-Champaign, Urban, IL 61801, USA. yi-lu@illinois.edu and Department of Biochemistry, University of Illinois at Urbana-Champaign, Urban, IL 61801, USA and Center for Biophysics and Quantitative Biology, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA and Carl R. Woese Institute for Genomic Biology, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.ORCID http://orcid.org/0000-0003-1221-6709
University of Illinois Urbana-Champaign · US

Funding

DESIGNING HETERONUCLEAR METALLOENZYMESR01GM062211 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI LU, YI · 2001 to 2021
$5.1M
Complementary Studies of Native Sulfite Reductase and Biosynthetic Model to Understand Structural Features Responsible for Selective Multi-Electron Reduction of SulfiteF32GM136177 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI REED, CHRISTOPHER (CHRIS) J · 2020 to 2022
$145k
NIGMS NIH HHS F32 GM136177NIGMS NIH HHS R01 GM062211
6 · The paper itself

Abstract

Heme-copper oxidases (HCO), nitric oxide reductases (NOR), and sulfite reductases (SiR) catalyze the multi-electron and multi-proton reductions of O2, NO, and SO32-, respectively. Each of these reactions is important to drive cellular energy production through respiratory metabolism and HCO, NOR, and SiR evolved to contain heteronuclear active sites containing heme/copper, heme/nonheme iron, and heme-[4Fe-4S] centers, respectively. The complexity of the structures and reactions of these native enzymes, along with their large sizes and/or membrane associations, make it challenging to fully understand the crucial structural features responsible for the catalytic properties of these active sites. In this review, we summarize progress that has been made to better understand these heteronuclear metalloenzymes at the molecular level though study of the native enzymes along with insights gained from biomimetic models comprising either small molecules or proteins. Further understanding the reaction selectivity of these enzymes is discussed through comparisons of their similar heteronuclear active sites, and we offer outlook for further investigations.

Indexed as

Biomimetic MaterialsCatalysisCatalytic DomainHemeMetalloproteinsModels, MolecularOxidation-ReductionOxidoreductasesOxidoreductases Acting on Sulfur Group DonorsProtein Conformationcopper oxidaseHemeMetalloproteinsnitric-oxide reductaseOxidoreductasesOxidoreductases Acting on Sulfur Group Donors

Identifiers

PMID33475096
PMCPMC7920998
OpenAlexW3123776560

What OpenQuestion holds

Textmetadata
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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.