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PubMed2001

Influence of Ni2+ and Co2+ on methanogenic activity and the amounts of coenzymes involved in methanogenesis.

The requirement of Ni2+ and Co2+ addition on methanogenic activity and the coenzymes involved in methanogenesis were investigated in anaerobic continuous cultivation with synthetic wastewater using acetate as the sole carbon source. Addition of Ni2+ and Co2+ to the synthetic wastewater drastically increased the maximum dilution rate of the cultivation. The concentrations of coenzymes F430 and corrinoids in the biomass increased to 0.62 micromol-Ni/g-VSS and 0.67 micromol-Co/g-VSS, respectively with the increase of the dilution rate. Methanogenic activity of the culture broth also increased with an increase of dilution rate. However, without addition of Ni2+ and Co2+, F430 and corrinoids were not detected in the biomass and methanogenic activity was only a trace level at a dilution rate of 0.025 d(-1). When the amounts of Ni2+ and Co2+ added at a dilution rate of 0.6 d(-1) were lowered in steps, the concentrations of F430 and corrinoids in the biomass and methanogenic activity decreased with decreasing amounts of Ni2+ and Co2+ added. These results suggest that Ni2+ and Co2+ were required for the methane-producing reactions via increases of coenzymes F430 and corrinoids.

Journal Article↗
PubMed2006

Anaerobic transformation of a technical brominated diphenyl ether mixture by super-reduced vitamin B12 and dicyanocobinamide.

The anaerobic transformation of the technical octabromo diphenyl ether mixture, DE-79, was investigated by incubation with two super-reduced corrinoids, dicyanocobinamide and cyanocobalamin (vitamin B12). The transformation produced 33 brominated diphenyl ethers (BDEs), 23 of which could be assigned to known structures. Within 1 d, the hepta- to nona-BDEs in DE-79 were almost quantitatively transformed with dicyanocobinamide to lower-brominated homologs. Along with the decrease of high-brominated congeners, concentrations of some tetra- to hexabromo congeners initially increased, followed by a decreasing or constant concentration during longer incubations. Super-reduced cyanocobalamin also was able to transform BDE congeners of DE-79. Whereas the transformation rates of hepta- to nona-BDEs of DE-79 by both corrinoids were comparable, tri- to hexa-BDEs were susceptible to further transformation by super-reduced cyanocobalamin. Incubation of DE-79 with either corrinoid produced significant amounts of BDE 49. Because this congener is found in small quantities in both penta- and octabromo technical BDE mixtures, it may be a suitable indicator for reductive debromination of higher-brominated BDEs. Isolated BDE 196 was incubated as well with super-reduced dicyanocobalamine. After 1 d, 13 BDEs could be detected, with BDE 153, BDE 100, and BDE 99 dominating. After 7 d, only tetra-BDEs or lower-brominated BDEs were detectable. It could be shown that reductive debromination by super-reduced corrinoids is a possible source for lower-brominated BDEs (i.e., BDE 47, BDE 99, BDE 153, and BDE 154). The patterns observed with our bench-scale study design demonstrate that anaerobic transformation in the presence of reducing agents can help to explain the occurrence of environmentally relevant BDE congeners (e.g., BDE 47, BDE 99, and BDE 153).

Bromine↗
PubMed1993

Cobalamin-mediated mercury methylation by Desulfovibrio desulfuricans LS.

The prominence of sulfate reducers in mercury biomethylation prompted the examination of the methyl carrier and mercury methylation activity of Desulfovibrio desulfuricans LS. There was a low degree of mercury tolerance and a high degree of methylation during fermentative growth; the opposite was true during sulfate reduction. During 2 days of fermentative growth, up to 37% of HgCl2 was methylated at 0.1 micrograms/ml, but only 1.5% was methylated at 10.0 micrograms/ml. Less than 1% of the added HgCl2 was methylated under sulfate-reducing conditions. D. desulfuricans LS radioimmunoassay results were positive for cobalamin. The addition of CoCl2 and benzimidazole to fermentative cultures increased methylation activity. From D. desulfuricans LS grown in the presence of (57)CoCl2, a corrinoid was extracted and purified. High-performance liquid chromatography analysis of the purified extract yielded a single peak with the retention time of cobalamin, and 97% of the (57)Co radioactivity was associated with this peak. Fast atom bombardment and UV and visible spectra of the isolated corrinoid matched those of cobalamin. When methylated with (14)CH3I, the isolated corrinoid methylated Hg(2+) with a 93.9% preservation of (14)C specific activity. We conclude that D. desulfuricans LS methylates mercury via cobalamin (vitamin B12). Under physiological conditions, the enzymatic catalysis of this reaction is likely.

Corrinoids↗
PubMed1988

Depletion of serum holotranscobalamin II. An early sign of negative vitamin B12 balance.

Preferential depletion of corrinoids on transcobalamin II (i.e., sharply reduced holo transcobalamin II (TC II)) occurs early in vitamin B12 deficiency. We measured corrinoids (Cor) and cobalamins (Cbl) on transcobalamins I and III (TC I + III) and on TC II. We also measured the unsaturated B12 binding capacities of transcobalamin I and III and TC II in serum from patients with B12 deficiency (N = 5) (with or without concurrent folate deficiency), with pernicious anemia in remission (N = 7) (1 month after therapy), and in several control groups including healthy volunteers (N = 6), hematologically normal elderly hospitalized patients (N = 5), and non-B12 nonfolate deficient anemic elderly hospitalized volunteers (N = 5). In B12 deficient patients, Cor = 177 +/- 92 pg/ml, Cbl = 56 +/- 20 pg/ml, TC II Cor = 1.0 +/- 2.2 pg/ml, and TC II Cbl = 4.4 +/- 4.9 pg/ml in contrast to pooled controls with Cor = 730 +/- 229, Cbl = 523 +/- 198, TC II Cor = 100 +/- 84, and TC II Cbl = 88 +/- 70 (all values expressed in picograms/milliliters). In pernicious anemia in remission, Cor = 505 +/- 138, Cbl = 294 +/- 77, TC II Cor = 80 +/- 31 and TC II Cbl = 37 +/- 36. TC II unsaturated B12 binding capacity was significantly higher in B12 deficient patients than in pooled controls. These data support that: (a) holo TC II is sharply depleted in untreated B12 deficiency; (b) normally, the only Cor on TC II are cobalamins; (c) in treated pernicious anemia, TC II appears to also bind non-cobalamin corrinoids; (d) continued malabsorption of vitamin B12 may result in reduced B12 on TC II within a month after the last parenteral therapy with 1000 micrograms of cyanocobalamin, and (e) TC II UBBC rises as B12 deficiency is developing. Further investigation is required for definitive delineation of whether sharply reduced Cor on TC II in untreated B12 deficiency can diagnose "true" B12 deficiency, in view of false positive or false negative results which occur in all serum B12 assays.

Adult↗
PubMed1992

Isolation of a 5-hydroxybenzimidazolyl cobamide-containing enzyme involved in the methyltetrahydromethanopterin: coenzyme M methyltransferase reaction in Methanobacterium thermoautotrophicum.

Formaldehyde conversion into methyl-coenzyme M involves (a) reaction of the substrate with 5,6,7,8-tetrahydromethanopterin (H4MPT) giving 5,10-methylene-H4MPT, followed by its reduction to 5-methyl-H4MPT and (b) transfer of the methyl group from the latter compound to coenzyme M. The reactions were studied in a resolved system from Methanobacterium thermoautotrophicum strain delta H. The first part (a) of the reactions was catalyzed by the 55% ammonium sulfate supernatant of cell-free extracts. The methyltransferase step (b) was dependent on an oxygen-sensitive enzyme, called methyltransferase a (MTa). Isolation of MTa was achieved by gel filtration on Sephacryl S-400. MTa was a high-molecular-weight complex of at least 2000 kDa and between 900 to 1500 kDa when purified in the absence and presence of the detergent CHAPS, respectively. The enzyme consisted of 100 kDa units composed of three subunits in an alpha beta gamma configuration with apparent molecular masses of 35, 33 and 31 kDa, respectively. The corrinoid, 5-hydroxybenzymidazolyl cobamide (B12HBI, Factor III) copurified with MTa and the latter contained 2 nmol B12HBI per mg protein. B12HBI present in MTa could be methylated under the appropriate conditions by 5-methyl-H4MPT. These findings suggest that the corrinoid is a prosthetic group of MTa. MTa may be homologous to the corrinoid membrane protein purified before from M. thermoautotrophicum strain Marburg (Schulz, H., Albracht, S.P.J., Coremans, J.M.C.C. and Fuchs, G. (1988) Eur. J. Biochem. 171, 589-597).

Cobamides↗
PubMed2004

Abiotic transformation of toxaphene by superreduced vitamin B12 and dicyanocobinamide.

Toxaphene is a complex organochlorine pesticide mixture, residues of which are widespread in the environment. Previous studies with the isolated bacterium Sulfurospirillum (formerly Dehalospirillum) multivorans resulted in an effective anaerobic biotransformation of toxaphene. Since the bacterium contains a corrinoid derivative in the active center of the tetrachloroethene dehalogenase, we attempted to use superreduced corrinoids for abiotic transformation of toxaphene. The two corrinoids studied were dicyanocobinamide and cyanocobalamin (vitamin B12). Superreduced dicyanocobinamide mediated a rapid transformation of toxaphene. More than 90% of the initial pool was transformed within 6 h. The transformation was nonselective, and even the most persistent metabolite in environmental samples, the so-called dead-end metabolite 2-exo,3-endo,6-exo,8,9,10-hexachlorobornane (B6-923 or Hx-Sed) was transformed within hours. Superreduced cyanocobalamin was also able to transform toxaphene albeit at significantly lower velocity. The lack of transformation products detectable in gas chromatograms of hexanes-extracted fractions of the assays suggests rapid, sequential dehalogenation and/or destruction of the C10-hydrocarbon backbone of the compounds of technical toxaphene.

Chromatography, Gas↗
PubMed1996

Organic Free Radical-Promoted Isomerization of alpha- and beta-Alkylcobinamides(1).

Anaerobic reaction of alpha- or beta-alkylcobinamides (alpha- or beta-RCbi(+)'s) with the corresponding alkyl free radical, R(*) (where R = CH(3), CH(3)CH(2), or CH(3)CH(2)OCH(2)CH(2)), generated by the Fenton reaction using Fe(2+) and an alkyl hydroperoxide, RC(CH(3))(2)OOH, causes isomerization and leads to mixtures of alpha- and beta-RCbi(+)'s. The reaction does not occur, however, under aerobic conditions or under anaerobic conditions in the presence of an excess of the free radical scavenger H-Tempo. In addition, alpha-CH(3)CH(2)Cbi(+) reacts with 50 molar equiv of tert-butyl hydroperoxide and Fe(2+) to give a mixture of alkylcobinamides that contains 6% alpha-CH(3)Cbi(+) and 94% beta-CH(3)Cbi(+), showing that multiple transalkylations occur. A Co(II)-induced isomerization and the S(H)2 mechanism are ruled out on the basis of the known reactivity of RCbi(+) and product analysis. A mechanism is proposed which involves a direct oxidative free radical displacement by an R(*) to the metal of RCbi(+) via a dialkylcobalt(IV) corrinoid species. Since the reaction leads to equilibration of the two diastereomers under mild conditions, it can be used to study the equilibria between diastereomeric RCbi(+)'s. Thus, the equilibrium for the diastereomeric ethyl-13-epicobinamides, in which the e propionamide side chain of the corrin ring has been epimerized from the alpha to the beta face of the corrinoid, lies significantly more toward the alpha diastereomer than that for the normal ethylcobinamides. This represents the most direct experimental evidence obtained to date that the corrin ring side chains control the relative steric accessibility of the two faces of the cobalt corrinoids.

Journal Article↗
PubMed1998

O-demethylase from Acetobacterium dehalogenans--substrate specificity and function of the participating proteins.

The ether-cleaving O-demethylase isolated from syringate-grown cells of Acetobacterium dehalogenans (formerly named strain MC) consists of four proteins, components A, B, C and D. The enzyme system converts only phenyl methyl ethers with a hydroxyl group in the ortho position to the methoxyl moiety. The presence of a carboxyl group in the aromatic compound was not required for O-demethylase reaction. Component B mediated the conversion of vanillate to 3,4-dihydroxybenzoate in the presence of the Ti(III)-reduced corrinoid-containing component A. After addition of component D and tetrahydrofolate, methyl tetrahydrofolate was formed from vanillate in stoichiometric amounts. Titanium(III) citrate as a reductant could be replaced by H2, methyl viologen or ferredoxin, partially purified hydrogenase, purified component C obtained from A. dehalogenans, and ATP. From these findings, it was deduced that component B serves as vanillate:corrinoid protein methyltransferase (methyltransferase I) mediating the methyl transfer from vanillate to the reduced corrinoid protein component A. Component D functions as methylcorrinoid protein:tetrahydrofolate transferase (methyltransferase II). The role of component C is probably that of an activating protein reversing accidental oxidation of the protein-bound cob(I)alamin to cob(II)alamin in the presence of ATP and reducing equivalents supplied by the enzymatic oxidation of hydrogen.

Amino Acid Sequence↗
PubMed1998

Activation and reaction kinetics of the dimethylamine/coenzyme M methyltransfer in Methanosarcina barkeri strain Fusaro.

Dimethylamine/5-hydroxybenzimidazolylcobamide methyltransferase (DMA-MT) from Methanosarcina barkeri Fusaro catalyzes (Vmax = 4700 nmol x min(-1) x mg(-1) protein; k(cat) = 7.8 s(-1)) the transfer of a methyl group from dimethylamine (apparent Km = 0.45 mM) to its corrinoid prosthetic group to yield monomethylamine (MMA) and the methylated enzyme. The product, MMA, is a competitive inhibitor of the reaction (apparent Ki = 5.5 mM). The methyl group bound to the corrinoid prosthetic group of DMA-MT is subsequently transferred to coenzyme M in a reaction mediated by methylcobalamin/coenzyme M methyltransferase isoenzyme II [MT2(II)], which binds with high affinity to DMA-MT (apparent Km = 0.22 microM). As isolated, DMA-MT is inactive, but it can enzymically be reactivated by methyltransferase activating protein (MAP), ATP, and hydrogenase. Apart from the established role in corrinoid activation, ATP was found to act as a powerful allosteric effector on the methyltransferase reaction. The results of kinetic studies, supported by the resolution of as-yet partially purified auxiliary protein fractions, demonstrate that DMA-MT, MT2(II), MAP, and hydrogenase are the only enzymic components involved in the dimethylamine/coenzyme M methyltransfer in M. barkeri Fusaro.

Adenosine Triphosphate↗
PubMed1984

Role of carbon monoxide dehydrogenase in the autotrophic pathway used by acetogenic bacteria.

Anaerobic acetogenic bacteria utilize a pathway of autotrophic growth that differs from any previously described. One part of the pathway involves the reduction of CO2 to formate and its subsequent conversion to the methyl moiety of methyltetrahydrofolate. The second part involves the formation of a one-carbon intermediate from CO, CO2 and H2, or the carboxyl of pyruvate and combination of the intermediate with CoA and methyltetrahydrofolate mediated by a corrinoid enzyme to yield acetyl-CoA. Our studies have been concerned with this latter portion of the pathway and we have proposed that a one-carbon intermediate is formed via carbon monoxide dehydrogenase. It remained possible, however, that the function of the CO dehydrogenase is to reduce the cobalt of the corrinoid enzyme to Co+, which is required for it to act as a methyl acceptor, and that the dehydrogenase is not involved directly in the formation of a C1 intermediate. All the enzymes required for the synthesis of acetyl-CoA from CO and methyltetrahydrofolate or from methyltetrahydrofolate and the carboxyl of pyruvate have now been purified. With these purified enzymes, it has been possible to show that CO dehydrogenase is essential for acetyl-CoA synthesis with CO as the substrate under conditions in which the cobalt of the corrinoid is reduced by other means. In addition, using pyruvate ferredoxin oxidoreductase, it has been shown that a 14C1-CO dehydrogenase complex is formed from [1-14C]pyruvate. Furthermore, [1-14C]acetyl-CoA was synthesized using the 14C1-CO dehydrogenase complex. Thus the evidence appears conclusive that CO dehydrogenase has a direct role in the formation of the carboxyl of acetyl-CoA.

Acetyl Coenzyme A↗
PubMed1996

Purification and properties of an enzyme involved in the ATP-dependent activation of the methanol:2-mercaptoethanesulfonic acid methyltransferase reaction in Methanosarcina barkeri.

In Methanosarcina barkeri the transfer of the methyl group from methanol to 2-mercaptoethanesulfonic acid is catalyzed by the concerted action of two methyltransferases. The first one is the corrinoid-containing methanol:5-hydroxybenzimidazolylcobamide methyltransferase (MT1), which binds the methyl group of methanol to its corrinoid prosthetic group. MT1 is only catalytically active when the cobalt atom of the corrinoid is present in the highly reduced Co(I) state. In the course of its purification and even during catalysis, MT1 becomes oxidatively inactivated. The enzyme, however, may be reductively reactivated by a suitable reducing system (hydrogen and hydrogenase), ATP, and an enzyme called methyltransferase activation protein (MAP). In order to elucidate its role in the reactivation process, MAP was purified to apparent homogeneity. The protein had an Mr = 60,000. Preincubation of the enzymic components involved with 8-azido-ATP or with ATP demonstrated MAP to be the primary site of action of ATP. In agreement herewith, the protein was autophosphorylated by [gamma-32P]ATP in a 1:1 stoichiometry. Phosphorylated MAP substituted for ATP in the activation of MT1, and the addition of increasing amounts of MAP phosphate resulted in a corresponding increase of active MT1. However, in the presence of limiting amounts of MAP, maximal activation of MT1 could be achieved during a lag phase provided ATP was present, indicating that MAP acts as a catalyst. This paper is the first to report on the presence, isolation, and function of a phosphorylated protein in a methanogenic archaeon.

Adenosine Diphosphate↗
PubMed1992

Enzymes Involved in Anaerobic Polyethylene Glycol Degradation by Pelobacter venetianus and Bacteroides Strain PG1.

In extracts of polyethylene glycol (PEG)-grown cells of the strictly anaerobically fermenting bacterium Pelobacter venetianus, two different enzyme activities were detected, a diol dehydratase and a PEG-degrading enzyme which was characterized as a PEG acetaldehyde lyase. Both enzymes were oxygen sensitive and depended on a reductant, such as titanium citrate or sulfhydryl compounds, for optimal activity. The diol dehydratase was inhibited by various corrinoids (adenosylcobalamin, cyanocobalamin, hydroxocobalamin, and methylcobalamin) by up to 37% at a concentration of 100 muM. Changes in ionic strength and the K ion concentration had only limited effects on this enzyme activity; glycerol inhibited the enzyme by 95%. The PEG-degrading enzyme activity was stimulated by the same corrinoids by up to 80%, exhibited optimal activity in 0.75 M potassium phosphate buffer or in the presence of 4 M KCI, and was only slightly affected by glycerol. Both enzymes were located in the cytoplasmic space. Also, another PEG-degrading bacterium, Bacteroides strain PG1, contained a PEG acetaldehyde lyase activity analogous to the corresponding enzyme of P. venetianus but no diol dehydratase. Our results confirm that corrinoid-influenced PEG degradation analogous to a diol dehydratase reaction is a common strategy among several different strictly anaerobic PEG-degrading bacteria.

Journal Article↗
PubMed1997

Alcoholic cirrhosis and cobalamin metabolism.

The cobalamin status of 27 patients suffering from alcoholic cirrhosis and 20 control subjects was analyzed. Plasma cobalamin (p < 0.005), total corrinoids (p < 0.005) and their analogs (p < 0.05) were all significantly elevated in the cirrhosis patients. These differences were due to increased haptocorrin (HC)-bound corrinoid (p < 0.02), which could be explained by a deficient hepatic clearance of cobalamin bound to HC. The increase in the concentration of true cobalamin was greater than that of its analogs. There were positive correlations between cholestasis (serum alkaline phosphatase) and plasma analog concentrations (p < 0.05), HC-bound cobalamin (p < 0.005) and total corrinoids bound to HC (p < 0.005). The plasma concentrations of the indicators of cobalamin deficiency, homocysteine (p < 0.05) and methylmalonic acid (p < 0.001), were increased, which could indicate poor cellular penetration of vitamin B12 or a defect in the activation of the two vitamin-B12-dependent enzymes.

5-Methyltetrahydrofolate-Homocysteine S-Methyltran↗
PubMedDate not supplied

[Manganese-dependent ribonucleotide reductase of Propionibacterium freudenreichii subsp. shermanii: partial purification, characterization, and role in DNA biosynthesis].

Like Lactobacillus leichmanii, Rhizobium meliloti, and Euglena gracilis, P. freudenreichii implicates cobalamin in DNA anabolism via adenosylcobalamin-dependent ribonucleotide reductase. However, in the absence of corrinoids, P. freudenreichii is able to synthesize DNA with the involvement of an alternative ribonucleotide reductase, which is independent of adenosylcobalamin. This enzyme is localized in both the cytoplasm (80% of activity) and the cytoplasmic membrane (20% of activity), being loosely bound to the latter. Experiments with crude ribonucleotide reductase isolated from extracts of corrinoid-deficient cells showed that manganese specifically stimulates this enzyme and that it is composed of two protein subunits, a feature that is typical of all metal-containing reductases activated by molecular oxygen. Low concentrations of manganese ions enhanced DNA synthesis in corrinoid-deficient manganese-limited cells. This effect was prevented by the addition of 80 mM hydroxyurea, a specific inhibitor of metal-containing aerobic ribonucleotide reductases. It was concluded that, in adenosylcobalamin-deficient P. freudenreichii cells, DNA synthesis is provided with deoxyribosyl precursors through the functioning of manganese-dependent aerobic ribonucleotide reductase composed of two subunits.

Cell Membrane↗
PubMed1994

B12: reminiscences and afterthoughts.

This paper describes some of the chemistry of synthetic corrinoids and corphinoids carried out at the ETH (Swiss Federal Institute of Technology) after the completion of the non-enzymic synthesis of vitamin B12 and attempts to delineate the interplay between mechanistic hypotheses, model studies and the experimental research in B12 biosynthesis which had spurred this work. The afterthoughts deal with why and how the work on corrinoids eventually led to an experimental involvement in the problem of a chemical aetiology of the structure of natural nucleic acids.

Corrinoids↗
PubMed1984

Reductive activation of methanol: 5-hydroxybenzimidazolylcobamide methyltransferase of Methanosarcina barkeri.

Methanol: 5-hydroxybenzimidazolylcobamide methyltransferase (MT1) from Methanosarcina barkeri, which is one of the enzymes responsible for the transmethylation from methanol to coenzyme M, was found to be activated in the presence of hydrogenase and ferredoxin. This activation was shown to involve a reduction of the bound corrinoid to the Co (I) level, and was demonstrated by spectrophotometry and chemical conversion of reduced MT1 to its methylated form. The reducing system of hydrogenase and ferredoxin was able to reduce dithiols, like dithiodiethanesulfonate and cystine to their monomers, in the presence of a corrinoid, which acts as an electron carrier. The ferredoxin was purified 133-fold and was tentatively identified on the basis of spectral properties and iron content of 3.8-4.0 atoms iron per molecule ferredoxin (12,000 daltons).

Corrinoids↗
PubMed1989

Spectroelectrochemical studies of the corrinoid/iron-sulfur protein involved in acetyl coenzyme A synthesis by Clostridium thermoaceticum.

An 88-kDa corrinoid/iron-sulfur protein (C/Fe-SP) is the methyl carrier protein in the acetyl-CoA pathway of Clostridium thermoaceticum. In previous studies, it was found that this C/Fe-SP contains (5-methoxybenzimidazolyl)cobamide and a [4Fe-4S]2+/1+ center, both of which undergo redox cycling during catalysis, and that the benzimidazole base is uncoordinated to the cobalt (base off) in all three redox states, 3+, 2+, and 1+ [Ragsdale, S.W., Lindahl, P.A., & Münck, E. (1987) J. Biol. Chem. 262, 14289-14297]. In this paper, we have determined the midpoint reduction potentials for the metal centers in this C/Fe-SP by electron paramagnetic resonance and UV-visible spectroelectrochemical methods. The midpoint reduction potentials for the Co3+/2+ and the Co2+/1 couples of the corrinoid were found to be 300-350 and -504 mV (+/- 3 mV) in Tris-HCl at pH 7.6, respectively. We also removed the (5-methoxybenzimidazolyl)cobamide cofactor from the C/Fe-SP and determined that its Co3+/2+ reduction potential is 207 mV at pH 7.6. The midpoint potential for the [4Fe-4S]2+/1+ couple in the C/Fe-SP was determined to be -523 mV (+/- 5 mV). Removal of this cluster totally inactivates the protein; however, there is little effect of cluster removal on the midpoint potential of the Co2+/1+ couple. In addition, removal of the cobamide has an insignificant effect on the midpoint reduction potential of the [4Fe-4S] cluster. A 27-kDa corrinoid protein (CP) also was studied since it contains (5-methoxybenzimidazolyl)cobamide in the base-on form.(ABSTRACT TRUNCATED AT 250 WORDS)

Acetyl Coenzyme A↗
PubMed2001

Structural and electronic properties of Co-corrole, Co-corrin, and Co-porphyrin.

A quantitative study of the structure and electronic properties of Co-corrole, Co-corrin, and Co-porphyrin, using density functional theory, is reported. The structure of each macrocycle is optimized, with no symmetry constraints, by considering different spin states. The ground-state structures and spin states (S = 1 for Co-corrole, S = 0 for Co-corrin and S = 1/2 for Co-porphyrin) are in good agreement with the experimental data available. The trends in the sizes of the coordination cavities upon varying the inner metal atom and/or the macrocycle are analyzed and compared with those for the Fe-porphyrin we studied previously. Our results reveal that most of the distortion of the Co-corrin core in the B12 coenzyme is due to the inherent properties of Co-corrin. Quite different behaviors are found between corrinoids and porphyrins upon varying the spin state. While an increase in the metal-nitrogen (M-N) distance with spin state occurs in the porphyrins, the corrinoids show little variation in the M-N distance and, in some cases, undergo small structural changes in the ring structure. These results aid in understanding the often discussed question of why nature has chosen corrin/porphyrin for carrying out the particular biological functions identified in the B12 coenzyme.

Cobalt↗