Unknown

Dataset Information

0

Characterization of Methyl- and Acetyl-Ni Intermediates in Acetyl CoA Synthase Formed during Anaerobic CO2 and CO Fixation.

ABSTRACT: The Wood-Ljungdahl Pathway is a unique biological mechanism of carbon dioxide and carbon monoxide fixation proposed to operate through nickel-based organometallic intermediates. The most unusual steps in this metabolic cycle involve a complex of two distinct nickel-iron-sulfur proteins: CO dehydrogenase and acetyl-CoA synthase (CODH/ACS). Here, we describe the nickel-methyl and nickel-acetyl intermediates in ACS completing the characterization of all its proposed organometallic intermediates. A single nickel site (Nip) within the A cluster of ACS undergoes major geometric and redox changes as it transits the planar Nip, tetrahedral Nip-CO and planar Nip-Me and Nip-Ac intermediates. We propose that the Nip intermediates equilibrate among different redox states, driven by an electrochemical-chemical (EC) coupling process, and that geometric changes in the A-cluster linked to large protein conformational changes control entry of CO and the methyl group.

SUBMITTER: Can M 

PROVIDER: S-EPMC10311460 | biostudies-literature | 2023 Jun

REPOSITORIES: biostudies-literature

Json Xml
altmetric image

Publications

Characterization of Methyl- and Acetyl-Ni Intermediates in Acetyl CoA Synthase Formed during Anaerobic CO<sub>2</sub> and CO Fixation.

Can Mehmet M   Abernathy Macon J MJ   Wiley Seth S   Griffith Claire C   James Christopher D CD   Xiong Jin J   Guo Yisong Y   Hoffman Brian M BM   Ragsdale Stephen W SW   Sarangi Ritimukta R  

Journal of the American Chemical Society 20230612 25

The Wood-Ljungdahl Pathway is a unique biological mechanism of carbon dioxide and carbon monoxide fixation proposed to operate through nickel-based organometallic intermediates. The most unusual steps in this metabolic cycle involve a complex of two distinct nickel-iron-sulfur proteins: CO dehydrogenase and acetyl-CoA synthase (CODH/ACS). Here, we describe the nickel-methyl and nickel-acetyl intermediates in ACS completing the characterization of all its proposed organometallic intermediates. A  ...[more]

Similar Datasets

Unknown An alcove at the acetyl-CoA synthase nickel active site is required for productive substrate CO binding and anaerobic carbon fixation.
| S-EPMC11321310 | biostudies-literature
Unknown Infrared and EPR spectroscopic characterization of a Ni(I) species formed by photolysis of a catalytically competent Ni(I)-CO intermediate in the acetyl-CoA synthase reaction.
| S-EPMC2932805 | biostudies-literature
Unknown Native iron reduces CO<sub>2</sub> to intermediates and end-products of the acetyl-CoA pathway.
| S-EPMC5969571 | biostudies-literature
Unknown A De Novo Designed Trimeric Metalloprotein as a Ni<sub>p</sub> Model of the Acetyl-CoA Synthase.
| S-EPMC10299331 | biostudies-literature
Unknown Structure of the alpha2epsilon2 Ni-dependent CO dehydrogenase component of the Methanosarcina barkeri acetyl-CoA decarbonylase/synthase complex.
| S-EPMC2474488 | biostudies-literature
Unknown A functional Ni-Ni-[4Fe-4S] cluster in the monomeric acetyl-CoA synthase from Carboxydothermus hydrogenoformans.
| S-EPMC327167 | biostudies-literature
Unknown X-ray Absorption Spectroscopy Reveals an Organometallic Ni-C Bond in the CO-Treated Form of Acetyl-CoA Synthase.
| S-EPMC5710745 | biostudies-literature
Unknown Mixed Valence {Ni<sup>2+</sup>Ni<sup>1+</sup>} Clusters as Models of Acetyl Coenzyme A Synthase Intermediates.
| S-EPMC11295191 | biostudies-literature
Unknown Thioester synthesis through geoelectrochemical CO<sub>2</sub> fixation on Ni sulfides.
| S-EPMC9814748 | biostudies-literature
Unknown Structure, function, and mechanism of the nickel metalloenzymes, CO dehydrogenase, and acetyl-CoA synthase.
| S-EPMC4002135 | biostudies-literature