Investigating the role of the strong field ligands in [FeFe] hydrogenase: spectroscopic and functional characterization of a semi-synthetic mono-cyanide active site.
Journal
Chemical science
ISSN: 2041-6520
Titre abrégé: Chem Sci
Pays: England
ID NLM: 101545951
Informations de publication
Date de publication:
28 Sep 2022
28 Sep 2022
Historique:
received:
22
04
2022
accepted:
05
08
2022
entrez:
2
11
2022
pubmed:
3
11
2022
medline:
3
11
2022
Statut:
epublish
Résumé
Artificial maturation of hydrogenases provides a path towards generating new semi-synthetic enzymes with novel catalytic properties. Here enzymes featuring a synthetic asymmetric mono-cyanide cofactor have been prepared using two different hydrogenase scaffolds. Their structure and reactivity was investigated in order to elucidate the design rationale behind the native di-cyanide cofactor, and by extension the second coordination sphere of the active-site pocket. Surprisingly, the choice of host enzyme was found to have a dramatic impact on reactivity. Moreover, the study shows that synthetic manipulations of the active-site can significantly increase inhibitor tolerance, as compared to native [FeFe] hydrogenase, while retaining the enzyme's native capacity for reversible catalysis.
Identifiants
pubmed: 36320473
doi: 10.1039/d2sc02271k
pii: d2sc02271k
pmc: PMC9516953
doi:
Types de publication
Journal Article
Langues
eng
Pagination
11058-11064Informations de copyright
This journal is © The Royal Society of Chemistry.
Déclaration de conflit d'intérêts
There are no conflicts to declare.
Références
J Am Chem Soc. 2019 Jul 17;141(28):11269-11285
pubmed: 31283209
J Am Chem Soc. 2007 Sep 19;129(37):11447-58
pubmed: 17722921
Chem Sci. 2020 Sep 21;11(47):12789-12801
pubmed: 34094474
Nature. 2013 Jul 4;499(7456):66-69
pubmed: 23803769
Biochemistry. 2009 Aug 25;48(33):7780-6
pubmed: 19634879
J Am Chem Soc. 2013 Mar 6;135(9):3633-9
pubmed: 23383865
Chem Commun (Camb). 2013 Aug 7;49(61):6840-2
pubmed: 23792933
Proc Natl Acad Sci U S A. 2016 Jul 26;113(30):8454-9
pubmed: 27432985
Nat Chem Biol. 2013 Oct;9(10):607-609
pubmed: 23934246
Chem Soc Rev. 2021 Feb 15;50(3):1668-1784
pubmed: 33305760
J Am Chem Soc. 2017 Feb 1;139(4):1440-1443
pubmed: 28075576
Nature. 2010 May 13;465(7295):248-51
pubmed: 20418861
J Am Chem Soc. 2022 Feb 2;144(4):1534-1538
pubmed: 35041427
J Biol Chem. 2012 Jan 6;287(2):1489-99
pubmed: 22110126
Angew Chem Int Ed Engl. 2018 May 4;57(19):5429-5432
pubmed: 29577535
J Am Chem Soc. 2018 Jan 24;140(3):1057-1068
pubmed: 29251926
Chem Sci. 2020 Sep 22;11(38):10313-10323
pubmed: 34123177
Chem Commun (Camb). 2021 Jan 18;57(6):713-720
pubmed: 33367317
Biochemistry. 2015 Feb 24;54(7):1474-83
pubmed: 25633077
Structure. 1999 Jan 15;7(1):13-23
pubmed: 10368269
J Am Chem Soc. 2020 Mar 25;142(12):5493-5497
pubmed: 32125830
J Am Chem Soc. 2021 Dec 8;143(48):20320-20325
pubmed: 34813699
Science. 2014 Jan 24;343(6169):424-7
pubmed: 24458644
Inorg Chem. 2020 Nov 16;59(22):16474-16488
pubmed: 33147959
Proc Natl Acad Sci U S A. 2019 Aug 6;116(32):15802-15810
pubmed: 31337676
J Am Chem Soc. 2017 Oct 25;139(42):15122-15134
pubmed: 28910086
J Am Chem Soc. 2009 Oct 21;131(41):14979-89
pubmed: 19824734
Angew Chem Int Ed Engl. 2018 Mar 1;57(10):2596-2599
pubmed: 29334424
Dalton Trans. 2017 Dec 12;46(48):16947-16958
pubmed: 29177350
Chem Rev. 2014 Apr 23;114(8):4081-148
pubmed: 24655035
Can J Microbiol. 1980 Oct;26(10):1214-23
pubmed: 7006765
Dalton Trans. 2016 Dec 6;45(48):19242-19248
pubmed: 27549900
J Am Chem Soc. 2017 Dec 20;139(50):18222-18230
pubmed: 29179539
Science. 1998 Dec 4;282(5395):1853-8
pubmed: 9836629
J Am Chem Soc. 2001 Feb 28;123(8):1596-601
pubmed: 11456758
Biochim Biophys Acta. 2013 Aug-Sep;1827(8-9):974-85
pubmed: 23507618