Active Intermediates in Copper Nitrite Reductase Reactions Probed by a Cryotrapping-Electron Paramagnetic Resonance Approach.
copper center
copper nitrite reductase
electron paramagnetic resonance
metalloenzymes
redox enzyme
Journal
Angewandte Chemie (International ed. in English)
ISSN: 1521-3773
Titre abrégé: Angew Chem Int Ed Engl
Pays: Germany
ID NLM: 0370543
Informations de publication
Date de publication:
10 08 2020
10 08 2020
Historique:
received:
07
04
2020
pubmed:
1
5
2020
medline:
17
3
2021
entrez:
1
5
2020
Statut:
ppublish
Résumé
Redox active metalloenzymes catalyse a range of biochemical processes essential for life. However, due to their complex reaction mechanisms, and often, their poor optical signals, detailed mechanistic understandings of them are limited. Here, we develop a cryoreduction approach coupled to electron paramagnetic resonance measurements to study electron transfer between the copper centers in the copper nitrite reductase (CuNiR) family of enzymes. Unlike alternative methods used to study electron transfer reactions, the cryoreduction approach presented here allows observation of the redox state of both metal centers, a direct read-out of electron transfer, determines the presence of the substrate/product in the active site and shows the importance of protein motion in inter-copper electron transfer catalyzed by CuNiRs. Cryoreduction-EPR is broadly applicable for the study of electron transfer in other redox enzymes and paves the way to explore transient states in multiple redox-center containing proteins (homo and hetero metal ions).
Identifiants
pubmed: 32352195
doi: 10.1002/anie.202005052
pmc: PMC7497095
doi:
Substances chimiques
Nitrite Reductases
EC 1.7.-
nitrite reductase, copper-containing
EC 1.7.2.1
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
13936-13940Subventions
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/N013980/1
Pays : United Kingdom
Informations de copyright
© 2020 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA.
Références
Proc Natl Acad Sci U S A. 2005 Aug 23;102(34):12041-6
pubmed: 16093314
Metallomics. 2017 Nov 15;9(11):1470-1482
pubmed: 28702572
Chem Rev. 2014 Apr 9;114(7):3659-853
pubmed: 24588098
Phys Chem Chem Phys. 2010;12(20):5353-68
pubmed: 21491657
Cell Mol Life Sci. 2000 Aug;57(8-9):1236-59
pubmed: 11028916
Nature. 2013 Apr 4;496(7443):123-6
pubmed: 23535590
Acc Chem Res. 2000 Oct;33(10):728-35
pubmed: 11041837
J Am Chem Soc. 2009 Jun 24;131(24):8614-9
pubmed: 19469533
J Am Chem Soc. 2001 Feb 21;123(7):1403-15
pubmed: 11456714
ACS Catal. 2019 Jul 5;9(7):6087-6099
pubmed: 32051772
J Am Chem Soc. 2008 Jan 30;130(4):1205-13
pubmed: 18179210
J Biol Chem. 2009 Sep 18;284(38):25973-83
pubmed: 19586913
IUCrJ. 2016 Jun 15;3(Pt 4):271-81
pubmed: 27437114
Nature. 2009 Aug 13;460(7257):823-30
pubmed: 19675642
Biophys Chem. 2003 Sep;105(2-3):667-80
pubmed: 14499926
Chem Commun (Camb). 2019 May 25;55(42):5863-5866
pubmed: 31049498
Biochem Biophys Res Commun. 2009 Sep 11;387(1):169-73
pubmed: 19591804
J Am Chem Soc. 2011 Sep 28;133(38):15085-93
pubmed: 21863850
J Mol Biol. 2008 Apr 25;378(2):353-61
pubmed: 18353369
FEBS J. 2012 Jun;279(12):2174-81
pubmed: 22536809
J Biol Inorg Chem. 2007 Nov;12(8):1119-27
pubmed: 17712582
Microbiol Mol Biol Rev. 1997 Dec;61(4):533-616
pubmed: 9409151
Angew Chem Int Ed Engl. 2020 Aug 10;59(33):13936-13940
pubmed: 32352195
Biochem J. 1997 Jun 1;324 ( Pt 2):511-6
pubmed: 9182711
J Am Chem Soc. 2006 Oct 11;128(40):13102-11
pubmed: 17017790
Proc Natl Acad Sci U S A. 2007 Mar 13;104(11):4315-20
pubmed: 17360521
Biochemistry. 2014 Oct 21;53(41):6511-9
pubmed: 25251261
Science. 2019 May 10;364(6440):566-570
pubmed: 31073062
Biochemistry. 1994 Mar 22;33(11):3171-7
pubmed: 8136351
Nature. 2009 Nov 5;462(7269):117-20
pubmed: 19890332
Biochemistry. 2011 May 17;50(19):4121-31
pubmed: 21469743
Microb Biotechnol. 2017 Nov;10(6):1457-1467
pubmed: 27696775
J Am Chem Soc. 2009 Jan 14;131(1):277-88
pubmed: 19053185