Over-expression of carbon monoxide dehydrogenase-I with an accessory protein co-expression: a key enzyme for carbon dioxide reduction

Inoue, Takahiro; Takao, Kyousuke; Fukuyama, Yuto; Yoshida, Takashi; Sako, Yoshihiko

doi:10.1080/09168451.2014.890027

Cited by 9 publications

(10 citation statements)

References 29 publications

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“…The third cluster contains 116 proteins, mostly found in methanogenic archaea (Methanomicrobia, Methanococci). The CooC-type cluster harbors 298 sequences and includes all CooC proteins shown to be involved in CODH maturation, such as CooC from R. rubrum (CooC Rr ) (26), CooC3 Ch (27), and CooC from Desulfovibrio vulgaris (CooC Dv ) (28). The CooC-type cluster also encompasses CooC1 from C. hydrogenoformans (CooC1 Ch ), which is a nickel-binding ATPase whose crystal structure has been determined (27,31).…”

Section: Cooc Proteins Can Be Divided Into Three Subgroups-mentioning

confidence: 99%

“…AcsF Mt has been described as an ATPase of unknown function whose involvement in CODH maturation of bifunctional ACS/CODH was postulated but not shown (27,33). The AcsF-type cluster also encompasses the gene product of cooC2 from C. hydrogenoformans, which we therefore named AcsF Ch .…”

Section: Cooc Proteins Can Be Divided Into Three Subgroups-mentioning

confidence: 99%

“…We suggest that enzymes clustered in the CooC-type group may act in the maturation of the [Ni4Fe4S] cluster of CODHs, whereas those that belong to the AcsF-type group, such as AcsF Ch and AcsF Mt , catalyze the MgATP and nickel-dependent maturation of the Ni,Ni-[4Fe4S] cluster of ACS. A possible division of selected CooC proteins in two classes has also been proposed based on a phylogenetic tree (27).…”

Section: Nickelmentioning

confidence: 99%

“…CODH activity in vivo depends on an ATPase termed CooC (25)(26)(27)(28). CooC belongs to the MinD-type ATPases, an enzyme family with diverse functions and a synapomorphic KGG signature in their Walker A motif (GKGGhGK(T/S)) containing a characteristic lysine residue (signature lysine) in addition to the P-loop lysine (29).…”

mentioning

confidence: 99%

“…Additional proteins support the maturation of the CODH in Rhodospirillum rubrum (25); however, these additional proteins are not conserved in bacteria outside the Rhodospirillaceae and may be functionally replaced by non-homologous isofunctional enzymes in other organisms. Although CooC was shown to mature monofunctional CODHs (25)(26)(27)(28), it was proposed that the homologous ATPase AcsF supports the assembly of the C-cluster in the bifunctional ACS-CODH complex in Moorella thermoacetica (33).…”

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confidence: 99%

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AcsF Catalyzes the ATP-dependent Insertion of Nickel into the Ni,Ni-[4Fe4S] Cluster of Acetyl-CoA Synthase

Gregg

Goetzl

Jeoung

et al. 2016

Journal of Biological Chemistry

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Acetyl-CoA synthase (ACS) catalyzes the reversible condensation of CO, CoA, and a methyl-cation to form acetyl-CoA at a unique Ni,Ni-[4Fe4S] cluster (the A-cluster). However, it was unknown which proteins support the assembly of the A-cluster. We analyzed the product of a gene from the cluster containing the ACS gene, cooC2 from Carboxydothermus hydrogenoformans, named AcsF Ch , and showed that it acts as a maturation factor of ACS. AcsF Ch and inactive ACS form a stable 2:1 complex that binds two nickel ions with higher affinity than the individual components. The nickel-bound ACS-AcsF Ch complex remains inactive until MgATP is added, thereby converting inactive to active ACS. AcsF Ch is a MinD-type ATPase and belongs to the CooC protein family, which can be divided into homologous subgroups. We propose that proteins of one subgroup are responsible for assembling the Ni,Ni-[4Fe4S] cluster of ACS, whereas proteins of a second subgroup mature the [Ni4Fe4S] cluster of carbon monoxide dehydrogenases.The cellular maturation of metalloenzymes, previously considered a spontaneous process in vivo, typically depends on a machinery of uptake, storage, processing, and delivery factors (1). How metalloenzymes mature has been investigated for some systems, revealing surprisingly complex maturation pathways (2-8). Enzymes containing nickel, although still relatively small in number, play critical roles in archaea, bacteria, and eukarya, through which they impact the global hydrogen (Ni,Fe-hydrogenase), nitrogen (urease), and carbon (acetylCoA synthase, carbon monoxide dehydrogenase, and methylCoM reductase) cycles (9). For most of these enzymes, we now have a good understanding of how nickel is incorporated into the active site (8, 10).The nickel-enzymes acetyl-CoA synthase (ACS) 2 and carbon monoxide dehydrogenase (CODH) are found in a variety of anaerobic microbes, including bacterial sulfate reducers, acetogens, and hydrogenogens, as well as archaeal methanogens and sulfate reducers, where they act as the prime CO 2 and CO converter (11)(12)(13)(14). ACS and CODH can be found as independent monofunctional enzymes in Carboxydothermus hydrogenoformans (15) but are typically found in other microorganisms as protein complexes: in acetogens ACS and CODH form a bifunctional (␣␤) 2 complex, whereas in methanogens they are part of a large (␣␤␥␦⑀) 8 multienzyme complex (11,13,15,16). CODHs catalyze the reversible reduction of CO 2 to CO at the C-cluster, in which a single nickel ion, embedded within a 3Fe-4S scaffold with an additional iron in exo, binds and activates CO and CO 2 for turnover (17)(18)(19). ACS catalyzes the reversible condensation of CO, CoA, and a methyl-cation donated by the methylated corrinoid iron-sulfur protein to form acetyl-CoA (13). ACS depends on a Ni,Ni-[4Fe4S] cluster (also called A-cluster) for activity, in which the two nickel ions have distinct coordinations: the nickel ion distal to the [4Fe4S] cluster (Ni d ) is coordinated by two amide nitrogen atoms and two cysteine thiolates within a Cys-X-Cys ...

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Section: Cooc Proteins Can Be Divided Into Three Subgroups-mentioning

confidence: 99%

Section: Cooc Proteins Can Be Divided Into Three Subgroups-mentioning

confidence: 99%

Section: Nickelmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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AcsF Catalyzes the ATP-dependent Insertion of Nickel into the Ni,Ni-[4Fe4S] Cluster of Acetyl-CoA Synthase

Gregg

Goetzl

Jeoung

et al. 2016

Journal of Biological Chemistry

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CODehydrogenase and Acetyl‐CoASynthase Assembly

Dobbek

2017

Encyclopedia of Inorganic and Bioinorganic Chemistry

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Ni,Fe‐containing carbon monoxide dehydrogenases (CODHs) and acetyl‐CoA synthases (ACSs) are ubiquitous among anaerobic bacteria and archaea. CODHs catalyze the reversible reduction of CO 2 with two electrons and two protons to CO and water. ACSs catalyze the reversible condensation of CO, coenzyme A, and a methyl cation to acetyl‐CoA, and both enzymes can occur in a monofunctional or as a stable bifunctional complex. Compared to what is known about the maturation of other Ni‐containing enzymes, how CODH and ACS mature is just beginning to emerge. Despite differences in active‐site metal content (CODH: 1xNi, 4xFe; ACS: 2xNi, 4xFe), architecture (CODH: Ni integrated in a NiFe 3 S 4 cubanoidal subcluster; ACS: two Ni next to a [4Fe4S] cluster), active‐site accessibility, and protein fold, both Ni,Fe‐clusters are matured by homologous ATPases of the MinD/Mrp‐family called CooC (CODH maturation) and AcsF (ACS maturation). CooC sustains the ATP‐dependent Ni insertion into the active‐site cluster of CODHs in the presence of physiological nickel concentrations. CooC can bind nickel at a GCXC motif in the dimer interface and ADP/ATP binding changes the coordination of nickel. AcsF forms a tight complex with Ni‐free ACS, together creating a binding platform for two nickel ions. The Ni‐loaded ACS–AcsF complex remains inactive until MgATP is added to it, resulting in fully active ACS. Details of the mechanisms and structures known to date are discussed in the chapter.

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Maturation of the [Ni–4Fe–4S] active site of carbon monoxide dehydrogenases

et al. 2018

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Nickel-containing enzymes are diverse in terms of function and active site structure. In many cases, the biosynthesis of the active site depends on accessory proteins which transport and insert the Ni ion. We review and discuss the literature related to the maturation of carbon monoxide dehydrogenases (CODH) which bear a nickel-containing active site consisting of a [Ni–4Fe–4S] center called the C-cluster. The maturation of this center has been much less studied than that of other nickel-containing enzymes such as urease and NiFe hydrogenase. Several proteins present in certain CODH operons, including the nickel-binding proteins CooT and CooJ, still have unclear functions. We question the conception that the maturation of all CODH depends on the accessory protein CooC described as essential for nickel insertion into the active site. The available literature reveals biological variations in CODH active site biosynthesis.

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Over-expression of carbon monoxide dehydrogenase-I with an accessory protein co-expression: a key enzyme for carbon dioxide reduction

Cited by 9 publications

References 29 publications

AcsF Catalyzes the ATP-dependent Insertion of Nickel into the Ni,Ni-[4Fe4S] Cluster of Acetyl-CoA Synthase

AcsF Catalyzes the ATP-dependent Insertion of Nickel into the Ni,Ni-[4Fe4S] Cluster of Acetyl-CoA Synthase

CODehydrogenase and Acetyl‐CoASynthase Assembly

Maturation of the [Ni–4Fe–4S] active site of carbon monoxide dehydrogenases

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