NDLI: Modeling carbon monoxide dehydrogenase/acetyl-CoA synthase (CODH/ACS): a trinuclear nickel complex employing deprotonated amides and bridging thiolates

Please wait, while we are loading the content...

Investigation of protonatable residues in Rhodothermus marinus caa 3 haem-copper oxygen reductase: comparison with Paracoccus denitrificans aa 3 haem-copper oxygen reductase

Axial ligand complexes of the Rhodnius nitrophorins: reduction potentials, binding constants, EPR spectra, and structures of the 4-iodopyrazole and imidazole complexes of NP4

Incorporation of either molybdenum or tungsten into formate dehydrogenase from Desulfovibrio alaskensis NCIMB 13491; EPR assignment of the proximal iron-sulfur cluster to the pterin cofactor in formate dehydrogenases from sulfate-reducing bacteria

NMR investigation of the heme electronic structure in deoxymyoglobin possessing a fluorinated heme

Effect of phosphate on bacterioferritin-catalysed iron(II) oxidation

Mechanistic studies of 1-aminocyclopropane-1-carboxylic acid oxidase: single turnover reaction

Characterization of the heme–histidine cross-link in cyanobacterial hemoglobins from Synechocystis sp. PCC 6803 and Synechococcus sp. PCC 7002

Nucleation of calcium oxalate crystals on an imprinted polymer surface from pure aqueous solution and urine

On the role of the axial ligand in heme proteins: a theoretical study

NMR-validated structural model for oxidized Rhodopseudomonas palustris cytochrome c 556

Electron transfer in crystals of the binary and ternary complexes of methylamine dehydrogenase with amicyanin and cytochrome c551i as detected by EPR spectroscopy

Modeling carbon monoxide dehydrogenase/acetyl-CoA synthase (CODH/ACS): a trinuclear nickel complex employing deprotonated amides and bridging thiolates

JBIC Journal of Biological Inorganic Chemistry : Volume 9, Issue 1, January 2004

JBIC Journal of Biological Inorganic Chemistry : Volume 8

JBIC Journal of Biological Inorganic Chemistry : Volume 7

JBIC Journal of Biological Inorganic Chemistry : Volume 6

JBIC Journal of Biological Inorganic Chemistry : Volume 5

JBIC Journal of Biological Inorganic Chemistry : Volume 4

JBIC Journal of Biological Inorganic Chemistry : Volume 3

JBIC Journal of Biological Inorganic Chemistry : Volume 2

Modeling carbon monoxide dehydrogenase/acetyl-CoA synthase (CODH/ACS): a trinuclear nickel complex employing deprotonated amides and bridging thiolates

Content Provider	Springer Nature Link
Author	Hatlevik, Øyvind Blanksma, Mary C. Mathrubootham, Vaidyanathan Arif, Atta M. Hegg, Eric L.
Copyright Year	2004
Abstract	Carbon monoxide dehydrogenase/acetyl-CoA synthase (CODH/ACS) utilizes a unique Ni-M bimetallic site in the biosynthesis of acetyl-CoA, where a square-planar Ni ion is coordinated to two thiolates and two deprotonated amides in a Cys-Gly-Cys motif. The identity of M is currently a matter of debate, although both Cu and Ni have been proposed. In an effort to model ACS’s unusual active site and to provide insight into the mechanism of acetyl-CoA formation and the role of each of the metals ions, we have prepared and structurally characterized a number of Ni(II)–peptide mimic complexes. The mononuclear complexes Ni(II) N,N’-bis(2-mercaptoethyl)oxamide (1), Ni(II) N,N′-ethylenebis(2-mercaptoacetamide) (2), and Ni(II) N,N′-ethylenebis(2-mercaptopropionamide) (3) model the Ni(Cys-Gly-Cys) site and can be used as synthons for additional multinuclear complexes. Reaction of 2 with MeI resulted in the alkylation of the sulfur atoms and the formation of Ni(II) N,N′-ethylenebis(2-methylmercaptoacetamide) (4), demonstrating the nucleophilicity of the terminal alkyl thiolates. Addition of Ni(OAc)2·4H2O to 3 resulted in the formation of a trinuclear species 5, while 2 crystallizes as an unusual paddlewheel complex (6) in the presence of nickel acetate. The difference in reactivity between the similar complexes 2 and 3 highlights the importance of ligand design when synthesizing models of ACS. Significantly, 5 maintains the key features observed in the active site of ACS, namely a square-planar Ni coordinated to two deprotonated amides and two thiolates, where the thiolates bridge to a second metal, suggesting that 5 is a reasonable structural model for this unique enzyme.
Starting Page	238
Ending Page	246
Page Count	9
File Format	PDF
ISSN	09498257
Journal	JBIC Journal of Biological Inorganic Chemistry
Volume Number	9
Issue Number	2
e-ISSN	14321327
Language	English
Publisher	Springer-Verlag
Publisher Date	2004-01-21
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Carbon monoxide dehydrogenase/acetyl-CoA synthase Deprotonated amide Nickel Thiolate
Content Type	Text
Resource Type	Article
Subject	Biochemistry Inorganic Chemistry

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

The metalloclusters of carbon monoxide dehydrogenase/acetyl-CoA synthase: a story in pictures

Crystallographic Characterization of the Carbonylated A-Cluster in Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase.

Autocatalytic activation of acetyl-CoA synthase

The Role of an Iron-Sulfur Cluster in an Enzymatic Methylation Reaction METHYLATION OF CO DEHYDROGENASE/ACETYL-CoA SYNTHASE BY THE METHYLATED CORRINOID IRON-SULFUR PROTEIN

Acetyl-coenzyme A synthase: the case for a Nip0-based mechanism of catalysis

Equilibrium dialysis study and mechanistic implications of coenzyme A binding to acetyl-CoA synthase/carbon monoxide dehydrogenase from Clostridium thermoaceticum

Evidence for Intersubunit Communication during Acetyl-CoA Cleavage by the Multienzyme CO Dehydrogenase/Acetyl-CoA Synthase Complex from Methanosarcina thermophila EVIDENCE THAT THE β SUBUNIT CATALYZES C–C AND C–S BOND CLEAVAGE

Nickel in Subunit β of the Acetyl-CoA Decarbonylase/Synthase Multienzyme Complex in Methanogens CATALYTIC PROPERTIES AND EVIDENCE FOR A BINUCLEAR Ni-Ni SITE

Crystallographic evidence for a CO/CO2 tunnel gating mechanism in the bifunctional carbon monoxide dehydrogenase/acetyl coenzyme A synthase from Moorella thermoacetica

Modeling carbon monoxide dehydrogenase/acetyl-CoA synthase (CODH/ACS): a trinuclear nickel complex employing deprotonated amides and bridging thiolates

Similar Documents

The metalloclusters of carbon monoxide dehydrogenase/acetyl-CoA synthase: a story in pictures

Crystallographic Characterization of the Carbonylated A-Cluster in Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase.

Autocatalytic activation of acetyl-CoA synthase

The Role of an Iron-Sulfur Cluster in an Enzymatic Methylation Reaction METHYLATION OF CO DEHYDROGENASE/ACETYL-CoA SYNTHASE BY THE METHYLATED CORRINOID IRON-SULFUR PROTEIN

Acetyl-coenzyme A synthase: the case for a Nip0-based mechanism of catalysis

Equilibrium dialysis study and mechanistic implications of coenzyme A binding to acetyl-CoA synthase/carbon monoxide dehydrogenase from Clostridium thermoaceticum

Evidence for Intersubunit Communication during Acetyl-CoA Cleavage by the Multienzyme CO Dehydrogenase/Acetyl-CoA Synthase Complex from Methanosarcina thermophila EVIDENCE THAT THE β SUBUNIT CATALYZES C–C AND C–S BOND CLEAVAGE

Nickel in Subunit β of the Acetyl-CoA Decarbonylase/Synthase Multienzyme Complex in Methanogens CATALYTIC PROPERTIES AND EVIDENCE FOR A BINUCLEAR Ni-Ni SITE

Crystallographic evidence for a CO/CO2 tunnel gating mechanism in the bifunctional carbon monoxide dehydrogenase/acetyl coenzyme A synthase from Moorella thermoacetica

Modeling carbon monoxide dehydrogenase/acetyl-CoA synthase (CODH/ACS): a trinuclear nickel complex employing deprotonated amides and bridging thiolates