Model Complexes for the Nip Site of Acetyl Coenzyme A Synthase/Carbon Monoxide (CO) Dehydrogenase: Structure, Electrochemistry, and CO Reactivity

Anirban Bhandari; Ram Chandra Maji; Saikat Mishra; Akhilesh Kumar; Suman Kumar Barman; Partha Pratim Das; Kamran B. Ghiassi; Marilyn M. Olmstead; Apurba K. Patra

doi:10.1021/acs.inorgchem.8b02276

Model Complexes for the Ni_p Site of Acetyl Coenzyme A Synthase/Carbon Monoxide (CO) Dehydrogenase: Structure, Electrochemistry, and CO Reactivity

Anirban Bhandari
, Ram Chandra Maji
, Saikat Mishra
, Akhilesh Kumar
, Suman Kumar Barman
, Partha Pratim Das
, Kamran B. Ghiassi
, Marilyn M. Olmstead
, Apurba K. Patra^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

10 Citations (Scopus)

Abstract

Aliphatic thiolato-S-bridged tri- and binuclear nickel(II) complexes have been synthesized and characterized as models for the Ni_p site of the A cluster of acetyl coenzyme A synthase (ACS)/carbon monooxide (CO) dehydrogenase. Reaction of the in situ formed N₂S^thiol donor ligands with [Ni(H₂O)₆](ClO₄)₂ afforded the trinuclear complexes [Ni{(L^Me(S))₂Ni}₂](ClO₄)₂·CH₃CN (1·CH₃CN) and [Ni{(L^Br(S))₂Ni}₂](ClO₄)₂·5H₂O (2·5H₂O) following self-assembly. Complexes 1 and 2 react with [Ni(dppe)Cl₂] and dppe [dppe = 1,2-bis(diphenylphosphino)ethane] to afford the binuclear [Ni(dppe)Ni(L^Me(S))₂](ClO₄)₂·2H₂O (3·2H₂O) and [Ni(dppe)Ni(L^Br(S))₂](ClO₄)₂·0.75O(C₂H₅)₂ [4·0.75O(C₂H₅)₂], respectively. The X-ray crystal structures of 1-4 revealed a central Ni^IIS₄ moiety in 1 and 2 and a Ni^IIP₂S₂ moiety in 3 and 4; both moieties have a square-planar environment around Ni and may mimic the properties of the Ni_p site of ACS. The electrochemical reduction of both terminal Ni^II ions of 1 and 2 occurs simultaneously, which is further confirmed by the isolation of [Ni{(L^Me(S))₂Ni(NO)}₂](ClO₄)₂ (5) and [Ni{(L^Br(S))₂Ni(NO)}₂](ClO₄)₂ (6) following reductive nitrosylation of 1 and 2. Complexes 5 and 6 exhibit ν_NO at 1773 and 1789 cm^-1, respectively. In the presence of O₂, both 5 and 6 transform to nitrite-bound monomers [(L^Me(S-S))Ni(NO₂)](ClO₄) (7) and [(L^Br(S-S))Ni(NO₂)](ClO₄)₂ (8). The nature of the ligand modification is evident from the X-ray crystal structure of 7. To understand the origin of multiple reductive responses of 1-4, complex [(L^Me(SMe))₂Ni](ClO₄)₂ (9) is considered. The central NiS₄ part of 1 is labile like the Ni_p site of ACS and can be replaced by phenanthroline. The treatment of CO to reduce 3 generates a 3_red-(CO)₂ species, as confirmed by Fourier transform infrared (ν_CO = 1997 and 2068 cm^-1) and electron paramagnetic resonance (g₁ = 2.18, g₂ = 2.13, g₃ = 1.95, and A^P = 30-80 G) spectroscopy. The CO binding to Ni^I of 3_red is relevant to the ACS activity.

Original language	English
Pages (from-to)	13713-13727
Number of pages	15
Journal	Inorganic Chemistry
Volume	57
Issue number	21
DOIs	https://doi.org/10.1021/acs.inorgchem.8b02276
Publication status	Published - 05-11-2018

All Science Journal Classification (ASJC) codes

Physical and Theoretical Chemistry
Inorganic Chemistry

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10.1021/acs.inorgchem.8b02276

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Bhandari, A., Chandra Maji, R., Mishra, S., Kumar, A., Barman, S. K., Das, P. P., Ghiassi, K. B., Olmstead, M. M., & Patra, A. K. (2018). Model Complexes for the Ni_p Site of Acetyl Coenzyme A Synthase/Carbon Monoxide (CO) Dehydrogenase: Structure, Electrochemistry, and CO Reactivity. Inorganic Chemistry, 57(21), 13713-13727. https://doi.org/10.1021/acs.inorgchem.8b02276

@article{f0c5764ad29442f2bdffb15d9009e8d1,

title = "Model Complexes for the Nip Site of Acetyl Coenzyme A Synthase/Carbon Monoxide (CO) Dehydrogenase: Structure, Electrochemistry, and CO Reactivity",

abstract = "Aliphatic thiolato-S-bridged tri- and binuclear nickel(II) complexes have been synthesized and characterized as models for the Nip site of the A cluster of acetyl coenzyme A synthase (ACS)/carbon monooxide (CO) dehydrogenase. Reaction of the in situ formed N2Sthiol donor ligands with [Ni(H2O)6](ClO4)2 afforded the trinuclear complexes [Ni\{(LMe(S))2Ni\}2](ClO4)2·CH3CN (1·CH3CN) and [Ni\{(LBr(S))2Ni\}2](ClO4)2·5H2O (2·5H2O) following self-assembly. Complexes 1 and 2 react with [Ni(dppe)Cl2] and dppe [dppe = 1,2-bis(diphenylphosphino)ethane] to afford the binuclear [Ni(dppe)Ni(LMe(S))2](ClO4)2·2H2O (3·2H2O) and [Ni(dppe)Ni(LBr(S))2](ClO4)2·0.75O(C2H5)2 [4·0.75O(C2H5)2], respectively. The X-ray crystal structures of 1-4 revealed a central NiIIS4 moiety in 1 and 2 and a NiIIP2S2 moiety in 3 and 4; both moieties have a square-planar environment around Ni and may mimic the properties of the Nip site of ACS. The electrochemical reduction of both terminal NiII ions of 1 and 2 occurs simultaneously, which is further confirmed by the isolation of [Ni\{(LMe(S))2Ni(NO)\}2](ClO4)2 (5) and [Ni\{(LBr(S))2Ni(NO)\}2](ClO4)2 (6) following reductive nitrosylation of 1 and 2. Complexes 5 and 6 exhibit νNO at 1773 and 1789 cm-1, respectively. In the presence of O2, both 5 and 6 transform to nitrite-bound monomers [(LMe(S-S))Ni(NO2)](ClO4) (7) and [(LBr(S-S))Ni(NO2)](ClO4)2 (8). The nature of the ligand modification is evident from the X-ray crystal structure of 7. To understand the origin of multiple reductive responses of 1-4, complex [(LMe(SMe))2Ni](ClO4)2 (9) is considered. The central NiS4 part of 1 is labile like the Nip site of ACS and can be replaced by phenanthroline. The treatment of CO to reduce 3 generates a 3red-(CO)2 species, as confirmed by Fourier transform infrared (νCO = 1997 and 2068 cm-1) and electron paramagnetic resonance (g1 = 2.18, g2 = 2.13, g3 = 1.95, and AP = 30-80 G) spectroscopy. The CO binding to NiI of 3red is relevant to the ACS activity.",

author = "Anirban Bhandari and \{Chandra Maji\}, Ram and Saikat Mishra and Akhilesh Kumar and Barman, \{Suman Kumar\} and Das, \{Partha Pratim\} and Ghiassi, \{Kamran B.\} and Olmstead, \{Marilyn M.\} and Patra, \{Apurba K.\}",

note = "Publisher Copyright: Copyright {\textcopyright} 2018 American Chemical Society.",

year = "2018",

month = nov,

day = "5",

doi = "10.1021/acs.inorgchem.8b02276",

language = "English",

volume = "57",

pages = "13713--13727",

journal = "Inorganic Chemistry",

issn = "0020-1669",

publisher = "American Chemical Society",

number = "21",

}

TY - JOUR

T1 - Model Complexes for the Nip Site of Acetyl Coenzyme A Synthase/Carbon Monoxide (CO) Dehydrogenase

T2 - Structure, Electrochemistry, and CO Reactivity

AU - Bhandari, Anirban

AU - Chandra Maji, Ram

AU - Mishra, Saikat

AU - Kumar, Akhilesh

AU - Barman, Suman Kumar

AU - Das, Partha Pratim

AU - Ghiassi, Kamran B.

AU - Olmstead, Marilyn M.

AU - Patra, Apurba K.

PY - 2018/11/5

Y1 - 2018/11/5

N2 - Aliphatic thiolato-S-bridged tri- and binuclear nickel(II) complexes have been synthesized and characterized as models for the Nip site of the A cluster of acetyl coenzyme A synthase (ACS)/carbon monooxide (CO) dehydrogenase. Reaction of the in situ formed N2Sthiol donor ligands with [Ni(H2O)6](ClO4)2 afforded the trinuclear complexes [Ni{(LMe(S))2Ni}2](ClO4)2·CH3CN (1·CH3CN) and [Ni{(LBr(S))2Ni}2](ClO4)2·5H2O (2·5H2O) following self-assembly. Complexes 1 and 2 react with [Ni(dppe)Cl2] and dppe [dppe = 1,2-bis(diphenylphosphino)ethane] to afford the binuclear [Ni(dppe)Ni(LMe(S))2](ClO4)2·2H2O (3·2H2O) and [Ni(dppe)Ni(LBr(S))2](ClO4)2·0.75O(C2H5)2 [4·0.75O(C2H5)2], respectively. The X-ray crystal structures of 1-4 revealed a central NiIIS4 moiety in 1 and 2 and a NiIIP2S2 moiety in 3 and 4; both moieties have a square-planar environment around Ni and may mimic the properties of the Nip site of ACS. The electrochemical reduction of both terminal NiII ions of 1 and 2 occurs simultaneously, which is further confirmed by the isolation of [Ni{(LMe(S))2Ni(NO)}2](ClO4)2 (5) and [Ni{(LBr(S))2Ni(NO)}2](ClO4)2 (6) following reductive nitrosylation of 1 and 2. Complexes 5 and 6 exhibit νNO at 1773 and 1789 cm-1, respectively. In the presence of O2, both 5 and 6 transform to nitrite-bound monomers [(LMe(S-S))Ni(NO2)](ClO4) (7) and [(LBr(S-S))Ni(NO2)](ClO4)2 (8). The nature of the ligand modification is evident from the X-ray crystal structure of 7. To understand the origin of multiple reductive responses of 1-4, complex [(LMe(SMe))2Ni](ClO4)2 (9) is considered. The central NiS4 part of 1 is labile like the Nip site of ACS and can be replaced by phenanthroline. The treatment of CO to reduce 3 generates a 3red-(CO)2 species, as confirmed by Fourier transform infrared (νCO = 1997 and 2068 cm-1) and electron paramagnetic resonance (g1 = 2.18, g2 = 2.13, g3 = 1.95, and AP = 30-80 G) spectroscopy. The CO binding to NiI of 3red is relevant to the ACS activity.

AB - Aliphatic thiolato-S-bridged tri- and binuclear nickel(II) complexes have been synthesized and characterized as models for the Nip site of the A cluster of acetyl coenzyme A synthase (ACS)/carbon monooxide (CO) dehydrogenase. Reaction of the in situ formed N2Sthiol donor ligands with [Ni(H2O)6](ClO4)2 afforded the trinuclear complexes [Ni{(LMe(S))2Ni}2](ClO4)2·CH3CN (1·CH3CN) and [Ni{(LBr(S))2Ni}2](ClO4)2·5H2O (2·5H2O) following self-assembly. Complexes 1 and 2 react with [Ni(dppe)Cl2] and dppe [dppe = 1,2-bis(diphenylphosphino)ethane] to afford the binuclear [Ni(dppe)Ni(LMe(S))2](ClO4)2·2H2O (3·2H2O) and [Ni(dppe)Ni(LBr(S))2](ClO4)2·0.75O(C2H5)2 [4·0.75O(C2H5)2], respectively. The X-ray crystal structures of 1-4 revealed a central NiIIS4 moiety in 1 and 2 and a NiIIP2S2 moiety in 3 and 4; both moieties have a square-planar environment around Ni and may mimic the properties of the Nip site of ACS. The electrochemical reduction of both terminal NiII ions of 1 and 2 occurs simultaneously, which is further confirmed by the isolation of [Ni{(LMe(S))2Ni(NO)}2](ClO4)2 (5) and [Ni{(LBr(S))2Ni(NO)}2](ClO4)2 (6) following reductive nitrosylation of 1 and 2. Complexes 5 and 6 exhibit νNO at 1773 and 1789 cm-1, respectively. In the presence of O2, both 5 and 6 transform to nitrite-bound monomers [(LMe(S-S))Ni(NO2)](ClO4) (7) and [(LBr(S-S))Ni(NO2)](ClO4)2 (8). The nature of the ligand modification is evident from the X-ray crystal structure of 7. To understand the origin of multiple reductive responses of 1-4, complex [(LMe(SMe))2Ni](ClO4)2 (9) is considered. The central NiS4 part of 1 is labile like the Nip site of ACS and can be replaced by phenanthroline. The treatment of CO to reduce 3 generates a 3red-(CO)2 species, as confirmed by Fourier transform infrared (νCO = 1997 and 2068 cm-1) and electron paramagnetic resonance (g1 = 2.18, g2 = 2.13, g3 = 1.95, and AP = 30-80 G) spectroscopy. The CO binding to NiI of 3red is relevant to the ACS activity.

UR - https://www.scopus.com/pages/publications/85055569183

UR - https://www.scopus.com/pages/publications/85055569183#tab=citedBy

U2 - 10.1021/acs.inorgchem.8b02276

DO - 10.1021/acs.inorgchem.8b02276

M3 - Article

C2 - 30339375

AN - SCOPUS:85055569183

SN - 0020-1669

VL - 57

SP - 13713

EP - 13727

JO - Inorganic Chemistry

JF - Inorganic Chemistry

IS - 21

ER -

Model Complexes for the Ni_p Site of Acetyl Coenzyme A Synthase/Carbon Monoxide (CO) Dehydrogenase: Structure, Electrochemistry, and CO Reactivity

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