Evidence map›Paper›PMID 35133385›Full record

ReviewFaraday discussions2022

Spiers Memorial Lecture: activating metal sites for biological electron transfer.

Edward I Solomon, Anex Jose

Open access · greenAbstract readReview
In one paragraph

Review in Faraday discussions, 2022. 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
0.4field-weighted citation impact, top 43% 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, 5 citations in OpenAlex.

  1. Electron transfer in biological systems.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024
    Review
  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 2 institutions in 1 country.

Edward I SolomonDepartment of Chemistry, Stanford University, Stanford, CA 94305, USA. solomone@stanford.edu.ORCID 0000-0003-0291-3199
Anex JoseDepartment of Chemistry, Stanford University, Stanford, CA 94305, USA. solomone@stanford.edu.ORCID 0000-0002-4924-7886
SLAC National Accelerator Laboratory · USStanford University · US

Funding

Structure/Function Correlations Over Copper EnzymesR01DK031450 · NIDDK · STANFORD UNIVERSITY · PI EDWARD I SOLOMON · 1986 to 2026
$8.7M
NIDDK NIH HHS R01 DK031450
6 · The paper itself

Abstract

Metal sites in biology often exhibit unique spectroscopic features that reflect novel geometric and electronic structures imposed by the protein that are key to reactivity. The blue copper active site involved in long range, rapid biological electron transfer is a classic example. This review presents an overview of both traditional and synchrotron based spectroscopic methods and their coupling to electronic structure calculations to understand the unique features of the blue copper active site, their contributions to function and the role of the protein in determining the geometric and electronic structure of the active site (called the "entatic state"). The relation of this active site to other biological electron transfer sites is further developed. In particular, ultrafast XFEL spectroscopy is used to evaluate the methionine-S-Fe bond in cytochrome

Indexed as

CopperElectronsElectron TransportMetalsModels, MolecularCopperMetals

Identifiers

PMID35133385
PMCPMC9117523
OpenAlexW4206764832

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.