Tripping the light fantastic in membrane redox biology: linking dynamic structures to function in ER electron transfer chains.
5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase
/ metabolism
Animals
Chemistry Techniques, Analytical
/ methods
Cytochrome P-450 Enzyme System
/ metabolism
Electron Transport
/ physiology
Endoplasmic Reticulum
/ metabolism
Intracellular Membranes
/ enzymology
Mammals
/ metabolism
Models, Molecular
NADP
/ metabolism
NADPH-Ferrihemoprotein Reductase
/ chemistry
Nitric Oxide Synthase
/ metabolism
Oxidation-Reduction
Protein Conformation
Structure-Activity Relationship
cytochrome P450
cytochrome P450 reductase
electron transfer chemistry
membrane protein
protein domain dynamics
Journal
The FEBS journal
ISSN: 1742-4658
Titre abrégé: FEBS J
Pays: England
ID NLM: 101229646
Informations de publication
Date de publication:
06 2019
06 2019
Historique:
received:
18
11
2018
revised:
16
12
2018
accepted:
15
01
2019
pubmed:
19
1
2019
medline:
6
5
2020
entrez:
19
1
2019
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 30657259
doi: 10.1111/febs.14757
pmc: PMC6563164
doi:
Substances chimiques
NADP
53-59-8
Cytochrome P-450 Enzyme System
9035-51-2
Nitric Oxide Synthase
EC 1.14.13.39
NADPH-Ferrihemoprotein Reductase
EC 1.6.2.4
5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase
EC 2.1.1.13
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
2004-2017Subventions
Organisme : UK Biotechnology and Biological Sciences Research Council
ID : BB/N013980/1
Pays : International
Informations de copyright
© 2019 The Authors. The FEBS Journal published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.
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