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

Nickel-dependent oligomerization of the alpha subunit of acetyl-coenzyme a synthase/carbon monoxide dehydrogenase. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Nickel-dependent oligomerization of the alpha subunit of acetyl-coenzyme a synthase/carbon monoxide dehydrogenase. Abstract Text:

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

After activation with NiCl2, the recombinant alpha subunit of the Ni-containing alpha2beta2 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 alpha subunit has two conformations (open and closed), and contains a novel [Fe4S4]-[Nip Nid] active site in which the proximal Nip ion is labile. Prior to Ni activation, recombinant apo-alpha contain only an Fe4S4 cluster. Ni-activated alpha subunits exhibit catalytic, spectroscopic and heterogeneity properties typical of alpha subunits contained in ACS/CODH. Evidence presented here indicates that apo-alpha is a monomer whereas Ni-treated alpha oligomerizes, forming dimers and higher molecular weight species including tetramers. No oligomerization occurred when apo-alpha was treated with Cu(II), Zn(II), or Co(II) ions, but oligomerization occurred when apo-alpha was treated with Pt(II) and Pd(II) ions. The dimer accepted only 0.5 methyl group/alpha and exhibited, upon treatment with CO and under reducing conditions, the NiFeC EPR signal quantifying to 0.4 spin/alpha. Dimers appear to consist of two types of alpha 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 alpha subunit, possibly to the open conformation, that promotes oligomerization. These interrelated events demonstrate previously unrealized connections between (a) the conformation of the alpha subunit; (b) the metal which occupies the proximal/distal sites of the A-cluster; and (c) catalytic activity.

Nickel-dependent oligomerization of the alpha subunit of acetyl-coenzyme a synthase/carbon monoxide dehydrogenase. Publishing Authors By Initials

X Tan,I Kagiampakis,IV Surovtsev,B Demeler,PA Lindahl,X Tan,I Kagiampakis,IV Surovtsev,B Demeler,PA Lindahl,X Tan,I Kagiampakis,IV Surovtsev,B Demeler,PA Lindahl,X Tan,I Kagiampakis,IV Surovtsev,B Demeler,PA Lindahl,

For similar abstracts research abstracts see: abstracts research

PUBMED ID PMID:

MEDLINE DATE:

Nickel-dependent oligomerization of the alpha subunit of acetyl-coenzyme a synthase/carbon monoxide dehydrogenase. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: Biochemistry

VOLUME: 46

Page Numbers: 11606-13

Journal Abbreviation: Biochemistry

ISSN: 0006-2960

DAY: 22

MONTH: 09

YEAR: 2007

Nickel-dependent oligomerization of the alpha subunit of acetyl-coenzyme a synthase/carbon monoxide dehydrogenase. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 370623

Nickel-dependent oligomerization of the alpha subunit of acetyl-coenzyme a synthase/carbon monoxide dehydrogenase. Keywords Mesh Terms:

KEYWORDS:

MESH TERMS:

Chemical & Substance for Abstract: Nickel-dependent oligomerization of the alpha subunit of acetyl-coenzyme a synthase/carbon monoxide dehydrogenase. Information

Substance Name:

Registry Number:

Grant and Affiliation Information for Nickel-dependent oligomerization of the alpha subunit of acetyl-coenzyme a synthase/carbon monoxide dehydrogenase.

AFFILIATION: Department of Chemistry, Texas A&M University, College Station, Texas 77843, USA.

Country: United States

AGENCY: United States NCI

GRANT: P30 CA054174

ACRONYM: CA

MEDLINETA: Biochemistry

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Nickel-dependent oligomerization of the alpha subunit of acetyl-coenzyme a synthase/carbon monoxide dehydrogenase Related Publications

• 2,5-Dihydroxybenzoic acid instead of alpha-cyano-4-hydroxycinnamic acid as matrix in matrix-assisted laser desorption/ionization time-of-flight mass spectrometry for analyses of in-gel digests of silver-stained proteins.
• A New Cryo-EM Single-Particle Ab Initio Reconstruction Method Visualizes Secondary Structure Elements in an ATP-Fueled AAA+ Motor.
• Adaptation of human embryonic stem cells to feeder-free and matrix-free culture conditions directly on plastic surfaces.
• Cartilage as a target tissue for growth hormone and insulin-like growth factor I.
• Constitutive and 3-methylcholanthrene-induced rat ALDH3A1 expression is mediated by multiple xenobiotic response elements.
• Effect of Zn on acetyl coenzyme a synthase: evidence for a conformational change in the alpha subunit during catalysis.
• Electron paramagnetic resonance and Mössbauer spectroscopy of intact mitochondria from respiring Saccharomyces cerevisiae.
• Epidemiology of periprosthetic femur fracture around a total hip arthroplasty.
• Experimental skin pain induced by injection of water-soluble substances in humans.
• Inactivation of acetyl-CoA synthase/carbon monoxide dehydrogenase by copper.
• Kinetics of CO insertion and acetyl group transfer steps, and a model of the acetyl-CoA synthase catalytic mechanism.
• Malignant melanotic progonoma. One case.
• Membrane proteins from the cyanobacterium Synechocystis sp. PCC 6803 interacting with thioredoxin.
• Mutations in the gene encoding the 3'-5' DNA exonuclease TREX1 cause Aicardi-Goutières syndrome at the AGS1 locus.
• Nickel-dependent oligomerization of the alpha subunit of acetyl-coenzyme a synthase/carbon monoxide dehydrogenase.
• Nonimmunodominant regions are effective as building blocks in a streptococcal fusion protein vaccine.
• Normal-mode analysis of the glycine alpha1 receptor by three separate methods.
• Not Available
• On the chlorine content of human muscle and skeletal tissue, with special reference to the degeneration of cartilage.
• On the chlorine content of human muscle and skeletal tissue, with special reference to the degeneration of cartilage.
• Persistent cardiac troponin I elevation in stabilized patients after an episode of acute coronary syndrome predicts long-term mortality.
• Prostate cancer detection with an improved resonance sensor system: parameter evaluation in a silicone model and on human prostate tissue in vitro.
• Reduction and methyl transfer kinetics of the alpha subunit from acetyl coenzyme a synthase.
• Rehabilitation in neurology.
• Safety of a topically applied metaflumizone spot-on formulation for flea control in cats and kittens.
• Safety of a topically applied spot-on formulation of metaflumizone plus amitraz for flea and tick control in dogs.
• Selecting thioredoxins for disulphide proteomics: Target proteomes of three thioredoxins from the cyanobacterium Synechocystis sp. PCC 6803.
• Spatial variations in prostate tissue histology as measured by a tactile resonance sensor.
• ULTRASONIC TREATMENT OF MENI'ERE'S DISEASE.
• [In Process Citation]