title: Synthetic Active Site Model of the [NiFeSe] Hydrogenase.
abstract: A dinuclear synthetic model of the [NiFeSe] hydrogenase active site and a structural, spectroscopic and electrochemical analysis of this complex is reported. [NiFe('S2Se2')(CO)3] (H2'S2Se2' = 1,2-bis(2-thiabutyl-3,3-dimethyl-4-selenol)benzene) has been synthesized by reacting the nickel selenolate complex [Ni('S2Se2')] with [Fe(CO)3bda] (bda = benzylideneacetone). X-ray crystal structure analysis confirms that [NiFe('S2Se2')(CO)3] mimics the key structural features of the enzyme active site, including a doubly bridged heterobimetallic nickel and iron center with a selenolate terminally coordinated to the nickel center. Comparison of [NiFe('S2Se2')(CO)3] with the previously reported thiolate analogue [NiFe('S4')(CO)3] (H2'S4' = H2xbsms = 1,2-bis(4-mercapto-3,3-dimethyl-2-thiabutyl)benzene) showed that the selenolate groups in [NiFe('S2Se2')(CO)3] give lower carbonyl stretching frequencies in the IR spectrum. Electrochemical studies of [NiFe('S2Se2')(CO)3] and [NiFe('S4')(CO)3] demonstrated that both complexes do not operate as homogenous H2 evolution catalysts, but are precursors to a solid deposit on an electrode surface for H2 evolution catalysis in organic and aqueous solution.
authors.affiliation: Christian Doppler Laboratory for Sustainable SynGas Chemistry, Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW (UK) http://www-reisner.ch.cam.ac.uk/
authors.forename: Claire
authors.initials: C
authors.lastname: Wombwell
authors.affiliation: Christian Doppler Laboratory for Sustainable SynGas Chemistry, Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW (UK) http://www-reisner.ch.cam.ac.uk/. reisner@ch.cam.ac.uk.
authors.forename: Erwin
authors.initials: E
authors.lastname: Reisner
mesh_terms: D040761:Biomimetic Materials / Q000737:chemistry*; D002384:Catalysis; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D006864:Hydrogenase / Q000737:chemistry*; D008958:Models, Molecular
chemical_list: C058560:nickel-iron-selenium hydrogenase; D006864:Hydrogenase
keywords: active sites; enzyme models; hydrogenase; selenium; structural models
references.citation: J Am Chem Soc. 2012 Dec 26;134(51):20745-55
references.pmid: 23194246
references.citation: J Am Chem Soc. 2014 Nov 5;136(44):15473-6
references.pmid: 25325406
references.citation: Nature. 1995 Feb 16;373(6515):580-7
references.pmid: 7854413
references.citation: Organometallics. 2014 Mar 24;33(6):1356-1366
references.pmid: 24748710
references.citation: J Am Chem Soc. 2009 Dec 30;131(51):18457-66
references.pmid: 19928857
references.citation: J Am Chem Soc. 2008 Oct 8;130(40):13410-6
references.pmid: 18781742
references.citation: Chem Rev. 2014 Apr 23;114(8):4081-148
references.pmid: 24655035
references.citation: Chem Commun (Camb). 2013 Aug 14;49(63):7061-3
references.pmid: 23811828
references.citation: J Biol Inorg Chem. 2010 Nov;15(8):1285-92
references.pmid: 20669037
references.citation: Inorg Chem. 2010 Nov 15;49(22):10338-47
references.pmid: 20964310
references.citation: Chem Commun (Camb). 2013 May 14;49(39):4331-3
references.pmid: 22918295
references.citation: Chemistry. 2009 Sep 21;15(37):9350-64
references.pmid: 19670195
references.citation: J Biol Inorg Chem. 2005 Oct;10(6):667-82
references.pmid: 16187073
references.citation: J Mol Biol. 2010 Mar 5;396(4):893-907
references.pmid: 20026074
references.citation: Structure. 2005 Nov;13(11):1635-42
references.pmid: 16271886
references.citation: J Bacteriol. 2006 May;188(9):3228-35
references.pmid: 16621815
references.citation: Angew Chem Int Ed Engl. 2014 Oct 20;53(43):11538-42
references.pmid: 25205168
references.citation: Structure. 1999 May;7(5):549-56
references.pmid: 10378274
references.citation: J Am Chem Soc. 2005 Jun 29;127(25):8950-1
references.pmid: 15969562
references.citation: J Am Chem Soc. 2014 Dec 3;136(48):16817-23
references.pmid: 25244613
references.citation: J Am Chem Soc. 2012 Apr 11;134(14):6479-90
references.pmid: 22424175
references.citation: Biochemistry. 1994 Aug 9;33(31):9229-36
references.pmid: 8049224
references.citation: J Am Chem Soc. 2014 Sep 24;136(38):13371-80
references.pmid: 25162793
references.citation: J Biol Inorg Chem. 2001 Jan;6(1):63-81
references.pmid: 11191224
references.citation: Inorg Chem. 2006 May 29;45(11):4334-6
references.pmid: 16711679
references.citation: Structure. 1999 May;7(5):557-66
references.pmid: 10378275
references.citation: Dalton Trans. 2014 Mar 21;43(11):4483-93
references.pmid: 24366040
references.citation: Angew Chem Weinheim Bergstr Ger. 2014 Oct 20;126(43):11722-11726
references.pmid: 26300567
references.citation: Chem Rev. 2007 Oct;107(10):4366-413
references.pmid: 17845060
references.citation: Science. 2013 Feb 8;339(6120):682-4
references.pmid: 23393260
references.citation: Chembiochem. 2013 Sep 23;14(14):1714-9
references.pmid: 24038675
references.citation: Nat Chem. 2009 Apr;1(1):7
references.pmid: 21378780
references.citation: Chem Commun (Camb). 2013 Jun 4;49(44):5004-6
references.pmid: 23612503
references.citation: J Am Chem Soc. 2014 Jul 16;136(28):10053-61
references.pmid: 24901378
references.citation: J Biol Inorg Chem. 2004 Sep;9(6):743-52
references.pmid: 15243788
references.citation: Chem Soc Rev. 2009 Jan;38(1):36-51
references.pmid: 19088963
references.citation: Biochemistry. 2006 Aug 15;45(32):9706-16
references.pmid: 16893172
references.citation: J Am Chem Soc. 2010 Oct 27;132(42):14877-85
references.pmid: 20925337
references.citation: Proc Natl Acad Sci U S A. 2005 Dec 20;102(51):18280-5
references.pmid: 16352727
references.citation: Nat Chem. 2014 Mar;6(3):248-53
references.pmid: 24557141
references.citation: Chemistry. 2015 Mar 2;21(10):3919-23
references.pmid: 25650832
references.citation: J Am Chem Soc. 2012 Apr 11;134(14):6104-7
references.pmid: 22458714
references.citation: J Am Chem Soc. 2012 May 23;134(20):8368-71
references.pmid: 22540997
references.citation: Chem Commun (Camb). 2010 Aug 28;46(32):5876-8
references.pmid: 20625582
references.citation: Science. 2004 Aug 13;305(5686):972-4
references.pmid: 15310892
references.citation: J Biosci Bioeng. 2013 Apr;115(4):366-71
references.pmid: 23201506
references.citation: J Biol Inorg Chem. 2002 Mar;7(3):318-26
references.pmid: 11935356
references.citation: Biochem Soc Trans. 2005 Feb;33(Pt 1):7-11
references.pmid: 15667250
references.citation: Biochim Biophys Acta. 2010 Feb;1797(2):304-13
references.pmid: 19925776
references.citation: Eur J Biochem. 1987 Aug 17;167(1):47-58
references.pmid: 3040402
references.citation: Biochemistry. 2013 Jan 8;52(1):4-18
references.pmid: 23240653
references.citation: Dalton Trans. 2008 Apr 28;(16):2128-35
references.pmid: 18398538
references.citation: Dalton Trans. 2009 Jun 14;(22):4304-9
references.pmid: 19662307
references.citation: J Biol Inorg Chem. 2013 Apr;18(4):419-27
references.pmid: 23468234
references.citation: Exp Cell Res. 2010 May 1;316(8):1296-303
references.pmid: 20206159
references.citation: Chem Commun (Camb). 2014 Nov 14;50(88):13514-6
references.pmid: 25237760
references.citation: J Biol Inorg Chem. 2005 May;10(3):239-49
references.pmid: 15803334
references.citation: J Biol Inorg Chem. 2012 Apr;17(4):543-55
references.pmid: 22286956
references.citation: Angew Chem Int Ed Engl. 2013 Nov 18;52(47):12313-6
references.pmid: 24115736