Total Synthesis of Acetate from CO<sub>2</sub>. I. Co-Methylcobyric Acid and Co-(Methyl)-5-methoxybenzimidazolylcobamide as Intermediates with Clostridium thermoaceticum<sup>*</sup>

Ljungdahl, Lars G.; Irion, E; Wood, Harland G.

doi:10.1021/bi00888a030

Cited by 109 publications

(57 citation statements)

References 19 publications

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“…It was shown for CoFeSP Mt from M. thermoacetica that the isolated cobamide contains a 5-methoxybenzimidazolyl group (8,14). The electron density for the bound cofactor in C. hydrogenoformans CoFeSP Ch shows the presence of two short groups at positions 5 and 6, indicating the presence of a dimethylbenzimidazolyl group (Fig.…”

Section: Resultsmentioning

confidence: 95%

Structural insights into methyltransfer reactions of a corrinoid iron–sulfur protein involved in acetyl-CoA synthesis

Svetlitchnaia¹,

Svetlitchnyi²,

Meyer

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

110

146

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acety-CoA pathway ͉ Carboxydothermus hydrogenoformans ͉ methyltransferase ͉ cobalt B 12-dependent enzymes are widespread in nature and catalyze distinct reactions. They can be grouped in three major classes: the isomerases, reductive dehalogenases, and methyltransferases (MeTrs; ref. 1). The cobalamin-dependent MeTrs play important roles in the amino acid biosynthesis in many organisms, ranging from bacteria to humans, as well as in the one-carbon metabolism of bacteria and archaea. MeTrs typically catalyze the transfer of methyl groups between organic and inorganic donors and acceptors like S-adenosylmethionine, methyltetrahydrofolate, and cobalamins. A unique methyltransfer reaction is found within the acetyl-CoA (Ljungdahl-Wood) pathway of autotrophic carbon assimilation, which operates in the anaerobic acetogenic, sulfidogenic, methanogenic, and hydrogenogenic bacteria and archaea. In the final step of the pathway, acetyl-CoA is synthesized from a methyl cation, carbon monoxide (CO), and CoA, a reaction catalyzed by the Ni-and Fe-containing enzyme acetyl-CoA synthase (ACS; for a review, see ref.2). Key to this reaction (Eq. 1) is the action of the Coand Fe-containing corrinoid iron-sulfur protein (CoFeSP) that donates the methyl group from methyl-cob(III)amide to one of the two Ni ions in the active site cluster A of ACS (3). This is the only methyltransfer reaction known with metals as donors and acceptors of the methyl group: CH 3 OCoFeSP ϩ CO ϩ CoA 3 CH 3 (CO)CoA ϩ CoFeSP. [1]CoFeSP has been isolated and characterized from the acetogenic bacterium Moorella thermoacetica (4), the methanogenic archaeon Methanosarcina thermophila (5), and the hydrogenogenic bacterium Carboxydothermus hydrogenoformans (6).C. hydrogenoformans can use CO as a sole source of energy and carbon under anaerobic chemolithoautotrophic conditions. Protons serve as terminal electron acceptor (7), and the methyl branch of the acetyl-CoA pathway is used for the assimilation of carbon (6). The oxidation of CO in this bacterium is catalyzed by two monofunctional NiFe-containing CODHs (CODHI Ch and CODHII Ch ) that harbor the [Ni-4Fe-5S] active site cluster C (7). A monomeric ACS Ch , a 1:1 molar complex of ACS Ch and CODHIII Ch , and CoFeSP Ch are expressed in functional form during the growth of C. hydrogenoformans using CO as the only substrate (6). The CoFeSP Ch from C. hydrogenoformans is a heterodimeric protein composed of a large subunit (48.4 kDa, CfsA) and a small subunit (33.9 kDa, CfsB) and harbors one molecule of the cobalt-containing corrinoid cofactor and a single The CoFeSPs from acetogens and methanogens are heterodimeric proteins sharing sequence identities of 35-53% with CoFeSP Ch from C. hydrogenoformans. CoFeSP Mt from M. thermoacetica was shown to contain two cofactors, 5-methoxybenzimidazolylcobamide (a variant of B12) and a [4Fe-4S] 2ϩ/1ϩ cluster, which gave the protein its name. For the cobamide cofactor, it was shown that neither the 5-methoxybenzimidazolyl group nor a nitrogen atom from a protein side chain is coor...

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Section: Resultsmentioning

confidence: 95%

Structural insights into methyltransfer reactions of a corrinoid iron–sulfur protein involved in acetyl-CoA synthesis

Svetlitchnaia¹,

Svetlitchnyi²,

Meyer

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

110

146

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“…Finally we will use this decomposition together with evidence from gene distributions to propose their historical relation and identify constraints that could have spanned the Darwinian and precellular eras. [90][91][92]94] consists of a sequence of five reactions that directly reduce one CO 2 to a methyl group, a parallel reaction reducing CO 2 to CO, and a final reaction combining the methyl and CO groups with each other and with a molecule of CoA to form the thioester acetyl-CoA. The reactions are shown below in figure 5, and discussed in detail in section 4.…”

Section: Core Carbon Metabolismmentioning

confidence: 99%

The compositional and evolutionary logic of metabolism

2012

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Metabolism is built on a foundation of organic chemistry, and employs structures and interactions at many scales. Despite these sources of complexity, metabolism also displays striking and robust regularities in the forms of modularity and hierarchy, which may be described compactly in terms of relatively few principles of composition. These regularities render metabolic architecture comprehensible as a system, and also suggests the order in which layers of that system came into existence. In addition metabolism also serves as a foundational layer in other hierarchies, up to at least the levels of cellular integration including bioenergetics and molecular replication, and trophic ecology. The recapitulation of patterns first seen in metabolism, in these higher levels, motivates us to interpret metabolism as a source of causation or constraint on many forms of organization in the biosphere. Many of the forms of modularity and hierarchy exhibited by metabolism are readily interpreted as stages in the emergence of catalytic control by living systems over organic chemistry, sometimes recapitulating or incorporating geochemical mechanisms. We identify as modules, either subsets of chemicals and reactions, or subsets of functions, that are re-used in many contexts with a conserved internal structure. At the small molecule substrate level, module boundaries are often associated with the most complex reaction mechanisms, catalyzed by highly conserved enzymes. Cofactors form a biosynthetically and functionally distinctive control layer over the small-molecule substrate. The most complex members among the cofactors are often associated with the reactions at module boundaries in the substrate networks, while simpler cofactors participate in widely generalized reactions. The highly tuned chemical structures of cofactors (sometimes exploiting distinctive properties of the elements of the periodic table) thereby act as 'keys' that incorporate classes of organic reactions within biochemistry. Module boundaries provide the interfaces where change is concentrated, when we catalogue extant diversity of metabolic phenotypes. The same modules that organize the compositional diversity of metabolism are argued, with many explicit examples, to have governed long-term evolution. Early evolution of core metabolism, and especially of carbon-fixation, appears to have required very few innovations, and to have used few rules of composition of conserved modules, to produce adaptations to simple chemical or energetic differences of environment without diverse solutions and without historical contingency. We demonstrate these features of metabolism at each of several levels of hierarchy, beginning with the small-molecule metabolic substrate and network architecture, continuing with cofactors and key conserved reactions, and culminating in the aggregation of multiple diverse physical and biochemical processes in cells.Content from this work may be used under the terms of the Creative Commons Attribution-NonCommercial-ShareAlike 3.0 licence.

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“…cell extract of M. thermoacetica (39 14 CH 3 -tetrahydrofolate to the methyl group of acetate. We then speculated that the conversion of Co-methylcorrinoids to acetate may occur via a Co-carboxymethylcorrinoid, which we synthesized and found to be converted to acetate by cell extracts.…”

Section: Total Biosynthesis Of Acetate From Carbon Dioxide By Moorellmentioning

confidence: 99%

A Life with Acetogens, Thermophiles, and Cellulolytic Anaerobes

Ljungdahl

2009

Annu. Rev. Microbiol.

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Frankly, I was surprised to receive an invitation to write a prefatory chapter for the Annual Review of Microbiology. I have read several such chapters written by outstanding researchers, many of whom I know and admire. I did not think I belonged to such a preeminent group. In my view, my contributions to the physiology and biochemistry of anaerobic thermophilic bacteria and, more lately, to anaerobic fungi are modest compared to the contribution made by other authors of prefatory chapters. I am honored to write about my life and my work, and I hope that those who read this chapter will sense how exciting and rewarding they have been.1

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Total Synthesis of Acetate from CO₂. I. Co-Methylcobyric Acid and Co-(Methyl)-5-methoxybenzimidazolylcobamide as Intermediates with Clostridium thermoaceticum^*

Cited by 109 publications

References 19 publications

Structural insights into methyltransfer reactions of a corrinoid iron–sulfur protein involved in acetyl-CoA synthesis

Structural insights into methyltransfer reactions of a corrinoid iron–sulfur protein involved in acetyl-CoA synthesis

The compositional and evolutionary logic of metabolism

A Life with Acetogens, Thermophiles, and Cellulolytic Anaerobes

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Total Synthesis of Acetate from CO2. I. Co-Methylcobyric Acid and Co-(Methyl)-5-methoxybenzimidazolylcobamide as Intermediates with Clostridium thermoaceticum*

Cited by 109 publications

References 19 publications

Structural insights into methyltransfer reactions of a corrinoid iron–sulfur protein involved in acetyl-CoA synthesis

Structural insights into methyltransfer reactions of a corrinoid iron–sulfur protein involved in acetyl-CoA synthesis

The compositional and evolutionary logic of metabolism

A Life with Acetogens, Thermophiles, and Cellulolytic Anaerobes

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Product

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Total Synthesis of Acetate from CO₂. I. Co-Methylcobyric Acid and Co-(Methyl)-5-methoxybenzimidazolylcobamide as Intermediates with Clostridium thermoaceticum^*