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Review
.2014:14:71-97.
doi: 10.1007/978-94-017-9269-1_4.

Investigations of the efficient electrocatalytic interconversions of carbon dioxide and carbon monoxide by nickel-containing carbon monoxide dehydrogenases

Affiliations
Review

Investigations of the efficient electrocatalytic interconversions of carbon dioxide and carbon monoxide by nickel-containing carbon monoxide dehydrogenases

Vincent C-C Wang et al. Met Ions Life Sci.2014.

Abstract

Carbon monoxide dehydrogenases (CODH) play an important role in utilizing carbon monoxide (CO) or carbon dioxide (CO2) in the metabolism of some microorganisms. Two distinctly different types of CODH are distinguished by the elements constituting the active site. A Mo-Cu containing CODH is found in some aerobic organisms, whereas a Ni-Fe containing CODH (henceforth simply Ni-CODH) is found in some anaerobes. Two members of the simplest class (IV) of Ni-CODH behave as efficient, reversible electrocatalysts of CO2/CO interconversion when adsorbed on a graphite electrode. Their intense electroactivity sets an important benchmark for the standard of performance at which synthetic molecular and material electrocatalysts comprised of suitably attired abundant first-row transition elements must be able to operate. Investigations of CODHs by protein film electrochemistry (PFE) reveal how the enzymes respond to the variable electrode potential that can drive CO2/CO interconversion in each direction, and identify the potential thresholds at which different small molecules, both substrates and inhibitors, enter or leave the catalytic cycle. Experiments carried out on a much larger (Class III) enzyme CODH/ACS, in which CODH is complexed tightly with acetyl-CoA synthase, show that some of these characteristics are retained, albeit with much slower rates of interfacial electron transfer, attributable to the difficulty in making good electronic contact at the electrode. The PFE results complement and clarify investigations made using spectroscopic investigations.

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Figures

Figure 1
Figure 1
Four different classes of anaerobic NiFe-containing CODH are classified by the subunit composition and biological roles. The Upper case letters denote the type of metal cluster. The A-cluster is the active site for acetyl-CoA synthesis. The C-cluster is the active site in which CO/CO2 conversion occurs. Several [Fe4S4] clusters are required for electron transfers in enzymes (B-cluster) and Class I and Class II enzymes have two additional [4Fe-4S] clusters (E and F clusters) in the enzyme complex. Co refers to the cobalt-corrinoid serving as a methyl carrier
Figure 2
Figure 2. CODES TO BE GIVEN
3D-structures of carbon monoxide dehydrogenases that have been studied by PFE.Upper left: CODH IICh showing how a relay of FeS clusters leads from the exposed D-cluster to two C-clusters, each one housed in one of the subunits.Lower left: same structure viewed facing up from the D-cluster.Right: CODH/ACS shown with the CODH viewed in same way as for lower-left view of CODH IICh.
Figure 3
Figure 3
The active site of CODH IICh seen through various crystal structures. (a) −600mV with CO2, (b) −320mV, (c) −320mV with cyanide and (d) CO-reduced CODH. Two positions are found for the dangling iron atom in the crystal structure, which is labelled Fe1a and Fe1b respectively. The pdb codes are shown in each case.
Figure 4
Figure 4
Concept of PFE, applied to CODH. Squares represent the FeS clusters D, B and C.
Figure 5
Figure 5
Electrocatalysis by carbon monoxide dehydrogenases adsorbed on a PGE rotating disk electrode in the presence of CO2 and CO. A. CODH ICh and CODH IICh under 50% CO and 50% CO2. Experimental Conditions: 25 °C, 0.2 M MES buffer (pH 7.0), electrode rotation rate 3500 rpm, and scan rate 2 mV s−1. Figure is reproduced from ref [19]. B.
Figure 6
Figure 6
A potential-domain dynamic picture of the effect of cyanide on catalytic properties of CODH.Left panels. Inhibition of CO oxidation activity of CODH ICh and CODH IICh by cyanide under 100 % CO. An aliquot of KCN stock solution (giving a final concentration of 1mM in the electrochemical cell) was injected during the second cycle. Conditions: 25 °C, 0.2 M MES buffer (pH=7.0), electrode rotation rate, 3500 rpm, scan rate, 1mV sec−1.Right panels. Inhibition of CO2 reduction activity of CODH ICh and CODH IICh by CN− under 100% CO2, showing that CN− does not bind under strongly reducing conditions. An aliquot of KCN stock solution (giving a final concentration of 1mM in the electrochemical cell) was injected during the second cycle. Note that a more negative potential (by approximately 70 mV) is required to reductively reactivate CODH IICh. Conditions: 25 °C, 0.2 M MES buffer (pH=7.0), electrode rotation rate, 3500 rpm, scan rate, 1mV sec−1.
Figure 5
Figure 5
Chronoamperometric measurements of the inactivation (Figure 5a and b) and re-activation (Figure 5c and d) rate of cyanide-inhibited CODH ICh and CODH IICh. The inactivation rate of CODH IICh by cyanide was measured at −460mV (CO oxidation, Figure 5a) and −560mV (CO2 reduction, Figure 5b). A final concentration of 0.5 mM cyanide in the electrochemical cell was used to measure the half-life time for inactivation. Cyanide release from CODH IICh (Figure 5d) at −760mV is much faster than the instrumental response. Conditions: 25 °C, 0.2 M MES buffer (pH=7.0), and rotation rate 3500 rpm.
Figure 8
Figure 8
Inhibition of CODH ICh by cyanate. Potassium cyanate was injected (final concentration in the solution is 6.67mM) into the electrochemical cell under gas atmosphere at 100% CO2 (Figure 3a) and 50% CO, 50% CO2 (Figure 3b). The experimental condition: 25°C, 0.2M MES buffer (pH=7.0), rotation rate 3500 rpm and scan rate 1mV s−1.
Figure 9
Figure 9
Reactions of carbon monoxide dehydrogenase with sulfide and thiocyanate.Upper. Cyclic voltammograms showing the reaction of CODH ICh and CODH IICh with sulfide: An aliquot of sodium sulfide stock solution (giving 1 mM final concentration) was injected into the electrochemical cell. Experimental conditions: 25 °C, 0.2 M MES buffer (pH 7.0), rotation rate 3500 rpm, scan rate: 1 mV s−1. Figure is reproduced from ref [64]Lower. Inhibition of CODH by thiocyanate. Thiocyanate was injected into the electrochemical cell to give a final concentration of 6.6 mM. Experimental conditions: 25 °C, 0.2 M MES buffer (pH 7.0), rotation rate 3500 rpm, scan rate: 1 mV s−1.
Figure 10
Figure 10
Potential dependence of binding of inhibitors to CODHICh.
Figure 11
Figure 11
Water gas shift reaction catalyzed by hydrogenase and CODH co-adsorbed on conducting graphite particles. Plot shows production of H2 and depeletion of CO over the course of 55 h, with fresh CO injections of 600 µL at the points indicated.
Figure 12
Figure 12
Upper. Cartoon showing a hybrid system for light-driven CO2 reduction using CODH on CdS nanoparticles. Numbers refer to potentials in V vs SHE.Lower. Comparison of the performance of CODH adsorbed on various CdS nanoparticles: NR = nanorods, QD = quantum dots, CdScalc = calcined sample. Adapted from Reference × with permission.
Figure 13
Figure 13
Cyclic voltammograms (scan rate 10 mV s−1) of electrocatalysis by CODH ICh adsorbed at PGE (upper), CdS thin film (middle) and TiO2 thin film (lower) electrodes, scanned in 0.2 M MES, pH 6.0. Voltammograms recorded under 100% CO2 are depicted in blue, and those recorded under 50% CO, 50% CO2 are shown in red.
Scheme 1
Scheme 1
Two possible mechanisms of Ni-Fe CODH proposed by (a) Dobbek and Lindahl, in which the Ni subsite in Cred2 is formally Ni(0) or (b) as proposed by Fontecilla-Camps et al[25], in which the Ni subsite in Cred2 is bonded to a H atom, making what is formally a Ni(II)-H species. The species ‘B’ refers to the amino acid that accepts/donates the proton, possibly His or Lys. The red colors represent substrate-mimic inhibitors in which cyanide (CN−) inhibits the Cred1 state and cyanate (NCO−) inhibits the Cred2 state.
Scheme 2
Scheme 2
Summary of the interceptions of the catalytic cycle of CODH by small molecule inhibitors. The potential −520 mV is the standard potential for the CO2/CO half cell reaction at pH 7.0. The potentials −50 mV and −250 mV are the values observed for re-activation of enzyme with and without sulfide. Reprinted from ref [65]
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