Evidence map›Paper›PMID 30657259›Full record

ReviewThe FEBS journal2019

Tripping the light fantastic in membrane redox biology: linking dynamic structures to function in ER electron transfer chains.

Tobias M Hedison, Nigel S Scrutton

Abstract readReview
In one paragraph

Review in The FEBS journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. Review
  2. A Review: Cytochrome P450 in Alcoholic and Non-Alcoholic Fatty Liver Disease.Diabetes, metabolic syndrome and obesity : targets and therapy · 2024
    Review
  3. Protein Dynamics and Enzymatic Catalysis.The journal of physical chemistry. B · 2023
    Review
  4. Roles of Ferredoxin-NADPAntioxidants (Basel, Switzerland) · 2022
    Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. 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.

Tobias M HedisonManchester Institute of Biotechnology and School of Chemistry, University of Manchester, UK.
Nigel S ScruttonManchester Institute of Biotechnology and School of Chemistry, University of Manchester, UK.

Funding

UK Biotechnology and Biological Sciences Research Council BB/N013980/1
6 · The paper itself

Abstract

How the dynamics of proteins assist catalysis is a contemporary issue in enzymology. In particular, this holds true for membrane-bound enzymes, where multiple structural, spectroscopic and biochemical approaches are needed to build up a comprehensive picture of how dynamics influence enzyme reaction cycles. Of note are the recent studies of cytochrome P450 reductases (CPR)-P450 (CYP) endoplasmic reticulum redox chains, showing the relationship between dynamics and electron flow through flavin and haem redox centres and the impact this has on monooxygenation chemistry. These studies have led to deeper understanding of mechanisms of electron flow, including the timing and control of electron delivery to protein-bound cofactors needed to facilitate CYP-catalysed reactions. Individual and multiple component systems have been used to capture biochemical behaviour and these have led to the emergence of more integrated models of catalysis. Crucially, the effects of membrane environment and composition on reaction cycle chemistry have also been probed, including effects on coenzyme binding/release, thermodynamic control of electron transfer, conformational coupling between partner proteins and vectorial versus 'off pathway' electron flow. Here, we review these studies and discuss evidence for the emergence of dynamic structural models of electron flow along human microsomal CPR-P450 redox chains.

Indexed as

5-Methyltetrahydrofolate-Homocysteine S-MethyltransferaseAnimalsChemistry Techniques, AnalyticalCytochrome P-450 Enzyme SystemElectron TransportEndoplasmic ReticulumIntracellular MembranesMammalsModels, MolecularNADPNADPH-Ferrihemoprotein ReductaseNitric Oxide SynthaseOxidation-ReductionProtein ConformationStructure-Activity Relationship5-Methyltetrahydrofolate-Homocysteine S-MethyltransferaseCytochrome P-450 Enzyme SystemNADPNADPH-Ferrihemoprotein ReductaseNitric Oxide Synthasecytochrome P450cytochrome P450 reductaseelectron transfer chemistrymembrane proteinprotein domain dynamics

Identifiers

PMID30657259
PMCPMC6563164

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.