Solution-State Inter-Copper Distribution of Redox Partner-Linked Copper Nitrite Reductases: A Pulsed Electron-Electron Double Resonance Spectroscopy Study.
Journal
The journal of physical chemistry letters
ISSN: 1948-7185
Titre abrégé: J Phys Chem Lett
Pays: United States
ID NLM: 101526034
Informations de publication
Date de publication:
04 Aug 2022
04 Aug 2022
Historique:
pubmed:
23
7
2022
medline:
6
8
2022
entrez:
22
7
2022
Statut:
ppublish
Résumé
Copper nitrite reductases (CuNiRs) catalyze the reduction of nitrite to form nitric oxide. In recent years, new classes of redox partner linked CuNiRs have been isolated and characterized by crystallographic techniques. Solution-state biophysical studies have shed light on the complex catalytic mechanisms of these enzymes and implied that protein dynamics may play a role in CuNiR catalysis. To investigate the structural, dynamical, and functional relationship of these CuNiRs, we have used protein reverse engineering and pulsed electron-electron double resonance (PELDOR) spectroscopy to determine their solution-state inter-copper distributions. Data show the multidimensional conformational landscape of this family of enzymes and the role of tethering in catalysis. The importance of combining high-resolution crystallographic techniques and low-resolution solution-state approaches in determining the structures and mechanisms of metalloenzymes is emphasized by our approach.
Identifiants
pubmed: 35867774
doi: 10.1021/acs.jpclett.2c01584
pmc: PMC9358711
doi:
Substances chimiques
Copper
789U1901C5
Nitrite Reductases
EC 1.7.-
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
6927-6934Références
Chemistry. 2016 Mar 24;22(14):4700-3
pubmed: 26865468
Magn Reson (Gott). 2020;1(2):209-224
pubmed: 34568875
Metallomics. 2017 Nov 15;9(11):1470-1482
pubmed: 28702572
Nature. 2007 Dec 13;450(7172):964-72
pubmed: 18075575
Methods Enzymol. 2015;563:531-67
pubmed: 26478498
J Phys Chem B. 2010 May 13;114(18):6165-74
pubmed: 20397677
J Mol Biol. 2003 Apr 25;328(2):429-38
pubmed: 12691751
J Am Chem Soc. 2007 Apr 25;129(16):4868-9
pubmed: 17394319
J Magn Reson. 2000 Feb;142(2):331-40
pubmed: 10648151
Proc Natl Acad Sci U S A. 2007 Mar 13;104(11):4315-20
pubmed: 17360521
J Magn Reson. 2002 Mar;155(1):72-82
pubmed: 11945035
Biochemistry. 1994 Mar 22;33(11):3171-7
pubmed: 8136351
J Magn Reson. 2006 Jan;178(1):42-55
pubmed: 16188474
ACS Catal. 2019 Jul 5;9(7):6087-6099
pubmed: 32051772
J Biol Chem. 2014 Apr 25;289(17):11725-11738
pubmed: 24610812
Angew Chem Int Ed Engl. 2020 Jun 8;59(24):9767-9772
pubmed: 32329172
Chem Commun (Camb). 2019 May 25;55(42):5863-5866
pubmed: 31049498
J Biol Inorg Chem. 2007 Nov;12(8):1119-27
pubmed: 17712582
Phys Chem Chem Phys. 2009 Aug 21;11(31):6580-91
pubmed: 19639133
Microbiol Mol Biol Rev. 1997 Dec;61(4):533-616
pubmed: 9409151
Nat Struct Mol Biol. 2017 Feb;24(2):187-193
pubmed: 28024148
Angew Chem Int Ed Engl. 2020 Aug 10;59(33):13936-13940
pubmed: 32352195
Nature. 2017 Mar 30;543(7647):738-741
pubmed: 28289287
Phys Chem Chem Phys. 2009 Aug 21;11(31):6840-8
pubmed: 19639159
Nature. 2013 Apr 4;496(7443):123-6
pubmed: 23535590
Sci Adv. 2018 Aug 24;4(8):eaat5218
pubmed: 30151430
Annu Rev Phys Chem. 2012;63:419-46
pubmed: 22404592
Science. 2019 May 10;364(6440):566-570
pubmed: 31073062
J Am Chem Soc. 2021 Nov 3;143(43):17875-17890
pubmed: 34664948
Phys Chem Chem Phys. 2016 Feb 17;18(8):5981-94
pubmed: 26837391
Angew Chem Int Ed Engl. 2013 Feb 11;52(7):1990-3
pubmed: 23296685
J Biol Chem. 2009 Sep 18;284(38):25973-83
pubmed: 19586913
Adv Protein Chem. 1991;42:145-97
pubmed: 1793005