Nickel-dependent oligomerization of the alpha subunit of acetyl-coenzyme A synthase/carbon monoxide dehydrogenase

Xiangshi Tan, Ioannis Kagiampakis, Ivan V. Surovtsev, Borries Demeler, Paul A. Lindahl

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

After activation with NiCl2, the recombinant α subunit of the Ni-containing α2β2 acetyl-CoA synthase/carbon monoxide dehydrogenase (ACS/CODH) catalyzes the synthesis of acetyl-CoA from CO, CoA, and a methyl group donated from the corrinoid-iron-sulfur protein (CoFeSP). The α subunit has two conformations (open and closed), and contains a novel [Fe4S 4]-[Nip Nid] active site in which the proximal Nip ion is labile. Prior to Ni activation, recombinant apo-α contain only an Fe4S4 cluster. Ni-activated α subunits exhibit catalytic, spectroscopic and heterogeneity properties typical of α subunits contained in ACS/CODH. Evidence presented here indicates that apo-α is a monomer whereas Ni-treated α oligomerizes, forming dimers and higher molecular weight species including tetramers. No oligomerization occurred when apo-α was treated with Cu(II), Zn(II), or Co(II) ions, but oligomerization occurred when apo-α was treated with Pt(II) and Pd(II) ions. The dimer accepted only 0.5 methyl group/α and exhibited, upon treatment with CO and under reducing conditions, the NiFeC EPR signal quantifying to 0.4 spin/α. Dimers appear to consist of two types of α subunits, including one responsible for catalytic activity and one that provides a structural scaffold. Higher molecular weight species may be similarly constituted. It is concluded that Ni binding to the A-cluster induces a conformational change in the α subunit, possibly to the open conformation, that promotes oligomerization. These interrelated events demonstrate previously unrealized connections between (a) the conformation of the α subunit; (b) the metal which occupies the proximal/distal sites of the A-cluster; and (c) catalytic activity.

Original languageEnglish (US)
Pages (from-to)11606-11613
Number of pages8
JournalBiochemistry
Volume46
Issue number41
DOIs
StatePublished - Oct 16 2007

Fingerprint

carbon monoxide dehydrogenase
Oligomerization
Acetyl Coenzyme A
Nickel
Dimers
Conformations
Ions
Carbon Monoxide
Catalyst activity
Catalytic Domain
Corrinoids
Molecular Weight
Chemical activation
Molecular weight
Iron-Sulfur Proteins
Coenzyme A
Scaffolds
Paramagnetic resonance
Monomers
Metals

ASJC Scopus subject areas

  • Biochemistry

Cite this

Tan, X., Kagiampakis, I., Surovtsev, I. V., Demeler, B., & Lindahl, P. A. (2007). Nickel-dependent oligomerization of the alpha subunit of acetyl-coenzyme A synthase/carbon monoxide dehydrogenase. Biochemistry, 46(41), 11606-11613. https://doi.org/10.1021/bi7014663

Nickel-dependent oligomerization of the alpha subunit of acetyl-coenzyme A synthase/carbon monoxide dehydrogenase. / Tan, Xiangshi; Kagiampakis, Ioannis; Surovtsev, Ivan V.; Demeler, Borries; Lindahl, Paul A.

In: Biochemistry, Vol. 46, No. 41, 16.10.2007, p. 11606-11613.

Research output: Contribution to journalArticle

Tan, X, Kagiampakis, I, Surovtsev, IV, Demeler, B & Lindahl, PA 2007, 'Nickel-dependent oligomerization of the alpha subunit of acetyl-coenzyme A synthase/carbon monoxide dehydrogenase', Biochemistry, vol. 46, no. 41, pp. 11606-11613. https://doi.org/10.1021/bi7014663
Tan, Xiangshi ; Kagiampakis, Ioannis ; Surovtsev, Ivan V. ; Demeler, Borries ; Lindahl, Paul A. / Nickel-dependent oligomerization of the alpha subunit of acetyl-coenzyme A synthase/carbon monoxide dehydrogenase. In: Biochemistry. 2007 ; Vol. 46, No. 41. pp. 11606-11613.
@article{ae47972279e641269c789cc58a61503f,
title = "Nickel-dependent oligomerization of the alpha subunit of acetyl-coenzyme A synthase/carbon monoxide dehydrogenase",
abstract = "After activation with NiCl2, the recombinant α subunit of the Ni-containing α2β2 acetyl-CoA synthase/carbon monoxide dehydrogenase (ACS/CODH) catalyzes the synthesis of acetyl-CoA from CO, CoA, and a methyl group donated from the corrinoid-iron-sulfur protein (CoFeSP). The α subunit has two conformations (open and closed), and contains a novel [Fe4S 4]-[Nip Nid] active site in which the proximal Nip ion is labile. Prior to Ni activation, recombinant apo-α contain only an Fe4S4 cluster. Ni-activated α subunits exhibit catalytic, spectroscopic and heterogeneity properties typical of α subunits contained in ACS/CODH. Evidence presented here indicates that apo-α is a monomer whereas Ni-treated α oligomerizes, forming dimers and higher molecular weight species including tetramers. No oligomerization occurred when apo-α was treated with Cu(II), Zn(II), or Co(II) ions, but oligomerization occurred when apo-α was treated with Pt(II) and Pd(II) ions. The dimer accepted only 0.5 methyl group/α and exhibited, upon treatment with CO and under reducing conditions, the NiFeC EPR signal quantifying to 0.4 spin/α. Dimers appear to consist of two types of α subunits, including one responsible for catalytic activity and one that provides a structural scaffold. Higher molecular weight species may be similarly constituted. It is concluded that Ni binding to the A-cluster induces a conformational change in the α subunit, possibly to the open conformation, that promotes oligomerization. These interrelated events demonstrate previously unrealized connections between (a) the conformation of the α subunit; (b) the metal which occupies the proximal/distal sites of the A-cluster; and (c) catalytic activity.",
author = "Xiangshi Tan and Ioannis Kagiampakis and Surovtsev, {Ivan V.} and Borries Demeler and Lindahl, {Paul A.}",
year = "2007",
month = "10",
day = "16",
doi = "10.1021/bi7014663",
language = "English (US)",
volume = "46",
pages = "11606--11613",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "American Chemical Society",
number = "41",

}

TY - JOUR

T1 - Nickel-dependent oligomerization of the alpha subunit of acetyl-coenzyme A synthase/carbon monoxide dehydrogenase

AU - Tan, Xiangshi

AU - Kagiampakis, Ioannis

AU - Surovtsev, Ivan V.

AU - Demeler, Borries

AU - Lindahl, Paul A.

PY - 2007/10/16

Y1 - 2007/10/16

N2 - After activation with NiCl2, the recombinant α subunit of the Ni-containing α2β2 acetyl-CoA synthase/carbon monoxide dehydrogenase (ACS/CODH) catalyzes the synthesis of acetyl-CoA from CO, CoA, and a methyl group donated from the corrinoid-iron-sulfur protein (CoFeSP). The α subunit has two conformations (open and closed), and contains a novel [Fe4S 4]-[Nip Nid] active site in which the proximal Nip ion is labile. Prior to Ni activation, recombinant apo-α contain only an Fe4S4 cluster. Ni-activated α subunits exhibit catalytic, spectroscopic and heterogeneity properties typical of α subunits contained in ACS/CODH. Evidence presented here indicates that apo-α is a monomer whereas Ni-treated α oligomerizes, forming dimers and higher molecular weight species including tetramers. No oligomerization occurred when apo-α was treated with Cu(II), Zn(II), or Co(II) ions, but oligomerization occurred when apo-α was treated with Pt(II) and Pd(II) ions. The dimer accepted only 0.5 methyl group/α and exhibited, upon treatment with CO and under reducing conditions, the NiFeC EPR signal quantifying to 0.4 spin/α. Dimers appear to consist of two types of α subunits, including one responsible for catalytic activity and one that provides a structural scaffold. Higher molecular weight species may be similarly constituted. It is concluded that Ni binding to the A-cluster induces a conformational change in the α subunit, possibly to the open conformation, that promotes oligomerization. These interrelated events demonstrate previously unrealized connections between (a) the conformation of the α subunit; (b) the metal which occupies the proximal/distal sites of the A-cluster; and (c) catalytic activity.

AB - After activation with NiCl2, the recombinant α subunit of the Ni-containing α2β2 acetyl-CoA synthase/carbon monoxide dehydrogenase (ACS/CODH) catalyzes the synthesis of acetyl-CoA from CO, CoA, and a methyl group donated from the corrinoid-iron-sulfur protein (CoFeSP). The α subunit has two conformations (open and closed), and contains a novel [Fe4S 4]-[Nip Nid] active site in which the proximal Nip ion is labile. Prior to Ni activation, recombinant apo-α contain only an Fe4S4 cluster. Ni-activated α subunits exhibit catalytic, spectroscopic and heterogeneity properties typical of α subunits contained in ACS/CODH. Evidence presented here indicates that apo-α is a monomer whereas Ni-treated α oligomerizes, forming dimers and higher molecular weight species including tetramers. No oligomerization occurred when apo-α was treated with Cu(II), Zn(II), or Co(II) ions, but oligomerization occurred when apo-α was treated with Pt(II) and Pd(II) ions. The dimer accepted only 0.5 methyl group/α and exhibited, upon treatment with CO and under reducing conditions, the NiFeC EPR signal quantifying to 0.4 spin/α. Dimers appear to consist of two types of α subunits, including one responsible for catalytic activity and one that provides a structural scaffold. Higher molecular weight species may be similarly constituted. It is concluded that Ni binding to the A-cluster induces a conformational change in the α subunit, possibly to the open conformation, that promotes oligomerization. These interrelated events demonstrate previously unrealized connections between (a) the conformation of the α subunit; (b) the metal which occupies the proximal/distal sites of the A-cluster; and (c) catalytic activity.

UR - http://www.scopus.com/inward/record.url?scp=35348883782&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=35348883782&partnerID=8YFLogxK

U2 - 10.1021/bi7014663

DO - 10.1021/bi7014663

M3 - Article

C2 - 17887777

AN - SCOPUS:35348883782

VL - 46

SP - 11606

EP - 11613

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 41

ER -