A Novel Pathway of Aerobic Benzoate Catabolism in the BacteriaAzoarcus evansii and Bacillus stearothermophilus

The aerobic catabolism of benzoate was studied in the Gram-negative proteobacterium Azoarcus evansii and in the Gram-positive bacterium Bacillus stearothermophilus. In contrast to earlier proposals, benzoate was not converted into hydroxybenzoate or gentisate. Rather, benzoyl-CoA was a product of benzoate catabolism in both microbial species under aerobic conditionsin vivo. Benzoyl-CoA was converted into various CoA thioesters by cell extracts of both species in oxygen- and NADPH-dependent reactions. Using [ring-13C6]benzoyl-CoA as substrate,cis-3,4-[2,3,4,5,6-13C5]dehydroadipyl-CoA,trans-2,3-[2,3,4,5,6-13C5]dehydroadipyl-CoA, the 3,6-lactone of 3-[2,3,4,5,6-13C5]hydroxyadipyl-CoA, and 3-[2,3,4,5,6-13C5]hydroxyadipyl-CoA were identified as products by NMR spectroscopy. A protein mixture ofA. evansii transformed [ring-13C6]benzoyl-CoA in an NADPH- and oxygen-dependent reaction into 6-[2,3,4,5,6-13C5]hydroxy-3-hexenoyl-CoA. The data suggest a novel aerobic pathway of benzoate catabolism via CoA intermediates leading to β-ketoadipyl-CoA, an intermediate of the known β-ketoadipate pathway. The aerobic catabolism of benzoate was studied in the Gram-negative proteobacterium Azoarcus evansii and in the Gram-positive bacterium Bacillus stearothermophilus. In contrast to earlier proposals, benzoate was not converted into hydroxybenzoate or gentisate. Rather, benzoyl-CoA was a product of benzoate catabolism in both microbial species under aerobic conditionsin vivo. Benzoyl-CoA was converted into various CoA thioesters by cell extracts of both species in oxygen- and NADPH-dependent reactions. Using [ring-13C6]benzoyl-CoA as substrate,cis-3,4-[2,3,4,5,6-13C5]dehydroadipyl-CoA,trans-2,3-[2,3,4,5,6-13C5]dehydroadipyl-CoA, the 3,6-lactone of 3-[2,3,4,5,6-13C5]hydroxyadipyl-CoA, and 3-[2,3,4,5,6-13C5]hydroxyadipyl-CoA were identified as products by NMR spectroscopy. A protein mixture ofA. evansii transformed [ring-13C6]benzoyl-CoA in an NADPH- and oxygen-dependent reaction into 6-[2,3,4,5,6-13C5]hydroxy-3-hexenoyl-CoA. The data suggest a novel aerobic pathway of benzoate catabolism via CoA intermediates leading to β-ketoadipyl-CoA, an intermediate of the known β-ketoadipate pathway. high performance liquid chromatography heteronuclear multiple quantum correlation spectroscopy total correlation spectroscopy The aerobic metabolism of benzoate (compound 1) (Fig.1) in bacteria has been studied in considerable detail (for a recent review, see Ref. 1Harwood C.S. Parales R.E. Annu. Rev. Microbiol. 1996; 50: 553-590Crossref PubMed Scopus (791) Google Scholar). Catechol (1,2-dihydroxybenzene, compound 3) and protocatechuate (3,4-dihydroxybenzoate, compound 2) were identified as early intermediates. Both compounds serve as substrates for dioxygenases that cleave the aromatic ring between the hydroxyl groups, leading to 3-ketoadipate (compound 4), which is converted into succinyl-CoA (compound 6) and acetyl-CoA (compound7) via compound 5 (ortho-cleavage pathway) (Fig. 1). However, some observations could not be explained by the established mechanisms. Thus, cell extracts of some Bacillus spp. grown on benzoate (compound 1) or 3-hydroxybenzoate (compound9) utilized gentisate (compound 11), but not catechol (compound 3) or protocatechuate (compound2) (Fig. 2). In an attempt to explain these findings, hydroxylation of benzoate (compound 1) affording 3-hydroxybenzoate (compound 9) (Fig.2) and gentisate (compound 11) was proposed (2Clark J.S. Buswell J.A. J. Gen. Microbiol. 1979; 112: 191-195Crossref Scopus (17) Google Scholar, 3Clark J.S. Buswell J.A. J. Gen. Microbiol. 1976; 96: 209-213Crossref PubMed Scopus (21) Google Scholar, 4Crawford R.L. J. Bacteriol. 1976; 127: 204-210Crossref PubMed Google Scholar). However, direct evidence for the suggested intermediates and reactions has not been obtained up to now. More recently, it was shown that the Gram-positive bacteriumBacillus stearothermophilus (5Kiemer P. Tshisuaka B. Fetzner S. Lingens F. Biol. Fertil. Soils. 1996; 23: 307-313Crossref Scopus (18) Google Scholar) and the facultative denitrifying Gram-negative bacterium Azoarcus evansii from the β-group of proteobacteria (6Anders J.H. Kaetzke A. Kämpfer P. Ludwig W. Fuchs G. Int. J. Syst. Bacteriol. 1995; 45: 327-333Crossref PubMed Scopus (254) Google Scholar, 7Braun K. Gibson D.T. Appl. Environ. Microbiol. 1984; 48: 102-107Crossref PubMed Google Scholar) are able to utilize benzoate (compound 1), 3-hydroxybenzoate (compound 9), or gentisate (compound 11) as the sole source of carbon and energy (5Kiemer P. Tshisuaka B. Fetzner S. Lingens F. Biol. Fertil. Soils. 1996; 23: 307-313Crossref Scopus (18) Google Scholar, 8Altenschmidt U. Oswald B. Steiner E. Herrmann H. Fuchs G. J. Bacteriol. 1993; 175: 4851-4858Crossref PubMed Google Scholar, 9Niemetz R. Altenschmidt U. Brucker S. Fuchs G. Eur. J. Biochem. 1995; 227: 161-168Crossref PubMed Scopus (23) Google Scholar). 2- and 4-hydroxybenzoate, protocatechuate, catechol, and 2,3-dihydroxybenzoate do not support growth (5Kiemer P. Tshisuaka B. Fetzner S. Lingens F. Biol. Fertil. Soils. 1996; 23: 307-313Crossref Scopus (18) Google Scholar, 8Altenschmidt U. Oswald B. Steiner E. Herrmann H. Fuchs G. J. Bacteriol. 1993; 175: 4851-4858Crossref PubMed Google Scholar). In conjunction with the presence of an aerobically inducible benzoate-CoA ligase (AMP-forming) and gentisate 1,2-dioxygenase, the degradation of benzoate was proposed to proceed via benzoyl-CoA (compound8) and either 2- or 3-hydroxybenzoyl-CoA (compound10) as intermediates (5Kiemer P. Tshisuaka B. Fetzner S. Lingens F. Biol. Fertil. Soils. 1996; 23: 307-313Crossref Scopus (18) Google Scholar, 8Altenschmidt U. Oswald B. Steiner E. Herrmann H. Fuchs G. J. Bacteriol. 1993; 175: 4851-4858Crossref PubMed Google Scholar). Further hydroxylation of either compound hypothetically could yield gentisyl-CoA, which might undergo thioester hydrolysis to gentisate (compound 11) (Fig. 2) (5Kiemer P. Tshisuaka B. Fetzner S. Lingens F. Biol. Fertil. Soils. 1996; 23: 307-313Crossref Scopus (18) Google Scholar,8Altenschmidt U. Oswald B. Steiner E. Herrmann H. Fuchs G. J. Bacteriol. 1993; 175: 4851-4858Crossref PubMed Google Scholar). However, the enzyme reactions catalyzing the proposed pathway to gentisate remained elusive. This report describes the conversion of [13C]benzoyl-CoA by cell extracts of A. evansii and B. stearothermophilus under aerobic conditions. Intermediates identified by NMR spectroscopy point to a gentisate-independent and hitherto unknown mechanism of aerobic benzoate degradation. [ring-14C]Benzoate was obtained from Amersham Pharmacia Biotech (Uppsala, Sweden), and [ring-13C6]benzoate was purchased from MSD Isotopes (Montreal, Canada). A. evansii KB740 (DSM6869) (6Anders J.H. Kaetzke A. Kämpfer P. Ludwig W. Fuchs G. Int. J. Syst. Bacteriol. 1995; 45: 327-333Crossref PubMed Scopus (254) Google Scholar) (formerly designated Pseudomonas sp. KB740) (7Braun K. Gibson D.T. Appl. Environ. Microbiol. 1984; 48: 102-107Crossref PubMed Google Scholar) was grown aerobically at 37 °C with benzoate or 3-hydroxybenzoate as the sole source of cell carbon and energy (8Altenschmidt U. Oswald B. Steiner E. Herrmann H. Fuchs G. J. Bacteriol. 1993; 175: 4851-4858Crossref PubMed Google Scholar, 14Tschech A. Fuchs G. Arch. Microbiol. 1987; 148: 213-217Crossref PubMed Scopus (235) Google Scholar) in a 200-liter fermentor (air flow, 100 liters/min; 200 rpm). Benzoate (10 mm) was added continuously when the initially added substrate (5 mm) was almost consumed. Cells were harvested in the exponential growth phase at an optical density (578 nm) of 2.3, corresponding to ∼0.6 g of cells (dry weight)/liter. The culture was cooled to 15 °C, and cells were harvested by continuous flow centrifugation. The yield was ∼200 g of cells (wet weight)/mol of benzoate. Alternatively, cells were grown in shaker flasks containing 5 mm 3-hydroxybenzoate. B. stearothermophilus PK1 (5Kiemer P. Tshisuaka B. Fetzner S. Lingens F. Biol. Fertil. Soils. 1996; 23: 307-313Crossref Scopus (18) Google Scholar) (courtesy of F. Lingens and J. Eberspächer, Universität Hohenheim) was grown at 56 °C in mineral salt medium (5Kiemer P. Tshisuaka B. Fetzner S. Lingens F. Biol. Fertil. Soils. 1996; 23: 307-313Crossref Scopus (18) Google Scholar) with benzoate (14 mm) as the sole source of cell carbon and energy in a 200-liter fermentor (air flow, 100 liters/min; 300 rpm). At an optical density (578 nm) of 1.2, the culture was cooled to 15 °C, and then cells were harvested by continuous flow centrifugation. Alternatively, cells were grown in 1-liter shaker flasks containing 400 ml of medium (150 rpm). All steps were performed at 4 °C. Frozen cells were suspended in an equal volume of water (A. evansii) or 200 mm Tris-HCl (pH 8) (B. stearothermophilus) containing 0.1 mg of DNase I/ml. The suspensions were passed through a French pressure cell at 123 megapascals and then centrifuged (100,000 × g). Benzoyl-CoA and 3-hydroxybenzoyl-CoA were prepared by published procedures (15Gross G.G. Zenk M.H. Z. Naturforschg. Sect. B. Chem. Sci. 1996; 21: 683-690Google Scholar, 18Schachter D. Taggart J.V. J. Biol. Chem. 1976; 203: 925-933Abstract Full Text PDF Google Scholar). The yield was 70–80%. [ring-13C6]Benzoyl-CoA was prepared by a slight modification of a published procedure (15Gross G.G. Zenk M.H. Z. Naturforschg. Sect. B. Chem. Sci. 1996; 21: 683-690Google Scholar). A reaction mixture containing 5 mmol of [ring-13C6]benzoate, 5 mmol ofN-hydroxysuccinimide, and 5 mmol of dicyclohexylcarbodiimide in 30 ml of dioxane was filtered, and the solvent was evaporated under reduced pressure. An aliquot of the succinimidyl ester (400 μmol) of the residue was dissolved in 1 ml of dioxane. Aliquots of 100 μl were added to 20 ml of 0.1 m sodium bicarbonate (pH 8) containing 200 μmol of coenzyme A. The reaction mixture was stirred at room temperature. Aliquots were retrieved at intervals, and thioester formation was monitored by the nitroprusside assay (16Stadtman E.R. Methods Enzymol. 1957; 3: 931-941Crossref Scopus (359) Google Scholar). After 1 h, the mixture was acidified to pH 3.5 by addition of 4 ml of 2 m formic acid and was then extracted with diethyl ether (3 × 50 ml). The aqueous phase was lyophilized. The residue was dissolved in 5 ml of 20 mm ammonium formate (pH 3.5) containing 2% (v/v) methanol (solvent 1). The solution was to a flow that been with the The was with ml of solvent 1 and then with (v/v) aqueous The was under reduced pressure and lyophilized. The yield was was prepared by a slight modification of a published U. Oswald B. Fuchs G. J. Bacteriol. PubMed Google Scholar). ml of 100 mm Tris-HCl (pH 8) containing 5 1 mm mm mm and 1 mm were added of of of and 1 of benzoate-CoA ligase from A. evansii U. Oswald B. Fuchs G. J. Bacteriol. PubMed Google Scholar). The reaction mixture was at 37 °C for and then acidified to pH 3.5 by addition of μl of (v/v) formic After × the was to a 1 flow that been with solvent The was with ml of solvent 1 and then with (v/v) aqueous The was under reduced pressure and lyophilized. The yield was Cells of A. evansii aerobically grown with benzoate were suspended in ml of mm Tris-HCl (pH 8) containing 1 mm and 1 mm gentisate. The was with for 5 at 37 °C. Aliquots were retrieved and added to 400 μl of The was centrifuged 4 and the was evaporated under reduced pressure at °C. The residue was dissolved in 50 μl of water and to an of (5 × 4 that been with 50 mm (pH (solvent 2) containing 2% (v/v) The was at a flow of 1 with 15 ml of solvent 2 containing 2% (v/v) then with ml of 50 mm (pH (solvent 3) containing (v/v) and with ml of a of (v/v) in solvent The was monitored with a and a were as unknown 2 and degradation product of In an attempt to the aerobic benzoate 5 mm or 5 mm or was added to the assay and for 20 at 37 °C to addition of 1 3-hydroxybenzoate and gentisate were not The steps were performed as pH containing mm mm and μl of cell extracts of or A. evansii mg of in Scholar) were stirred at °C. Aliquots were retrieved at The enzyme reaction was by 200 μl of protein was by centrifugation. The was evaporated under reduced pressure at °C, and the residue was dissolved in 100 μl of Aliquots of 30 μl were to a of (5 × 4 that been with solvent containing 2% (v/v) The was at a flow of 1 with ml of solvent containing 2% (v/v) and then with ml of a of (v/v) in solvent benzoyl-CoA was with ml of a of (v/v) in solvent The was monitored with the and the were as product product product and degradation product of were performed as was by mm) was was was by the assay with and was by were performed with in the presence of as and mm as After 5 the reaction was by addition of of protein was by centrifugation. Aliquots of 3.5 ml were to a of × 20 mm) that been with solvent containing 2% (v/v) The was at a flow of with 30 ml of solvent containing 2% (v/v) then with ml of a of (v/v) in solvent and with 30 ml of a of (v/v) in solvent were as product product product and degradation product of were The volume of the was reduced to 0.1 by at °C and The solution was lyophilized. The residue containing product 1 was dissolved in water containing (v/v) acid and (v/v) methanol (solvent and to a flow that been with solvent The was with ml of solvent 4 and then with ml of (v/v) aqueous The was under reduced pressure and lyophilized. The containing product 2 or were dissolved in water and to a 2 flow 0.1 that been with The was with ml of water and then with ml of (v/v) aqueous The solution was under reduced pressure and lyophilized. A protein benzoyl-CoA by was prepared from extracts from g of cells (wet ml of a cell of A. evansii g of cells (wet were to a 4 Amersham Pharmacia that been with mm Tris-HCl (pH (solvent at a flow of 3.5 The was with ml of solvent 5 and then with ml of solvent 5 containing mm The was with 200 ml of solvent 5 containing mm The was and was added to a of The solution mg of was at °C for 15 Aliquots of protein were to a of that been with solvent 5 at a flow of 1 The was with 30 ml of solvent 5 and ml of solvent 5 containing 2 mm sodium (pH the was with ml of solvent 5 containing 100 mm sodium (pH The was was added to a of and the solution mg of was at °C. containing ml of protein mm and 2 of were at °C for The reaction was by addition of ml of The mixture was centrifuged × 4 and the was to ml under reduced pressure. The solution was acidified to pH 5 by addition of 20 μl of (v/v) formic and of 100 μl were by as of compounds were as and product to product by NMR the acidified was a flow 0.1 that was with 20 mm ammonium formate (pH containing (v/v) (solvent The acidified was to the The was with ml of solvent and then with (v/v) The was to under reduced pressure containing mm 1 mm and ml of cell mg of of B. stearothermophilus were stirred at 20 °C. The of the was as for A. Aliquots of 30 μl were to a of (5 × 4 The was as for A. of products as as product product product product product and degradation product of were performed with containing as products were by as as for A. as product and product and 5 were 2 and 4 were The were as The were dissolved in ml of (pH 6) and NMR were at 20 °C a and and were performed to The of the was in the were performed with of cells of A. evansii were with mm) at room temperature. The mixture 3-hydroxybenzoate mm) and gentisate mm) to 3-hydroxybenzoate or gentisate. At intervals, of the mixture were and by as under and were The of gentisate was not gentisate is with After 15 a intermediate of the initially added with an of benzoyl-CoA was After the benzoyl-CoA intermediate and products which not to the of the intermediates with or 3-hydroxybenzoate was not that and gentisate do not serve as intermediates in the aerobic catabolism of benzoate in A. In an attempt to unknown cells ofA. evansii were with mm) and or (5 mm) in the of 3-hydroxybenzoate and gentisate. that and gentisate not However, the of product formation were In with cells of A. evansii that was not converted into 3-hydroxybenzoate or gentisate. Rather, benzoyl-CoA was as an of A. evansii cells were with or in the presence of mm) and (air Aliquots were retrieved at and by for the of CoA formation was not with as In products were when was as substrate More a of was to be to benzoate and coenzyme A to in the cell The of benzoyl-CoA was converted into products (Fig. and that from the at for CoA The product shown in was a pH of The products were and by as The of product 1 the compound of and a compound with a of of product 1 was converted into a novel compound shown NMR of the containing product 1 the presence of of product 2 at a of the of product a of at the of product 2 NMR that product was converted into product 2 and of products from mm) or mm) by cell extracts of A. evansii under for 5 at 37 mm mm of of products were by of the corresponding of the and are as of or initially product in a The of products were by of the corresponding of the and are as of or initially product the of substrate and product formation in After 5 of the initially added benzoyl-CoA was consumed. This was by the formation of the product 1 5 of the initially added and the formation of the products 2 and 1 and were in the of the product 2 not to be converted The of products from the on up to of the initially added The total to the formation of of mm) the catabolism of After 5 of benzoyl-CoA was with in the assay The product was to that in the assay at of the steps of benzoyl-CoA products were when was by mm) or when was product formation was on steps with extracts of A. evansii a protein mixture [ring-13C6]benzoyl-CoA into a product 6) by an NADPH- and oxygen-dependent was from the assay mixture by and by NMR spectroscopy. be that product was not in with cell extracts of A. the of the novel [ring-13C6]benzoyl-CoA mm) was in with cell extracts of A. evansii in the presence of mm) and A of was added to product and by After 5 the was when the of products were at The products were by and as under mg of products were obtained in and to NMR spectroscopy. The presence of CoA could be from the NMR for product not The NMR were by carbon that were from of More the NMR of the containing product 1 with of some with of the of and of the NMR were to compounds with and of compound and and of compound and to of compound were by to This evidence that the of substrate has been leading to which the of in the degradation as The were for or The could be from the from and In the carbon of compound was shown to be to and compound was established as be that of compound is to the of benzoyl-CoA and could not be by However, the of in compound the of a The of the of compound a However, of compound was from the corresponding of (compound In with compounds in data was as the 3,6-lactone of the NMR the of compounds and were as in the NMR data of products from by cell extracts of A. evansii and B. to from NMR to the are in in of compound compound 4), 3.5 compound 15 5 2 compound compound 4 to in from NMR to the are in in a of the NMR of product 2 and product that were with of product 2 was at a of for a acid and were at and carbon The of product was at a The as as the obtained from and the obtained from and (Fig. and established product 2 as (compound and product as (compound The NMR of in compound 20 was a with a of 15 of compound of and of product 2 compound obtained from with [ring-13C6]benzoyl-CoA and cell extracts of A. NMR data to that for product 2 (compound This might be explained by or 2) The conversion of [ring-13C6]benzoyl-CoA and by cell extracts of B. stearothermophilus was studied as for A. but in the presence of 1 mm was that the of early by a in the (Fig. and NMR identified the products as products 4 and (Fig. could be the of substrate and product formation in 4 was the of the products and was in the of the 2 and were More products The NMR of the containing products 2 and 4 that were to the NMR compound novel were to product 4 The NMR a In contrast to both of the to The carbon was by Thus, product 4 was as (compound A is suggested from the of the NMR of and The of product 5 was for NMR In that aerobic benzoate catabolism in A. evansii via benzoyl-CoA (compound8) and CoA but not via 3-hydroxybenzoate (compound 9), 3-hydroxybenzoyl-CoA (compound or gentisate (compound (compound the 3,6-lactone of (compound (compound were identified by NMR spectroscopy in aerobic reaction containing [ring-13C6]benzoyl-CoA and cell extracts of A. Using a protein of A. [ring-13C6]benzoyl-CoA was converted into (compound cell extracts of B. compounds (compound were were by the of the substrate to and of and with of of CoA The identified compounds be explained by (Fig. 1) or by suggested via gentisate (Fig. but point at a gentisate-independent novel pathway in the microbial species under A pathway of aerobic benzoate metabolism in A. evansii stearothermophilus the identified intermediates is shown in A. evansii and B. stearothermophilus to benzoate (compound 1) via coenzyme A The of the pathway is the formation of benzoyl-CoA (compound8) from benzoate (compound 1) and coenzyme A by a benzoate-CoA The formation of CoA of from [ring-13C6]benzoyl-CoA that and cleave the aromatic ring and that intermediates. A protein mixture obtained from extracts of A. steps converted benzoyl-CoA in an NADPH- and oxygen-dependent reaction into (compound compound or a compound to compound is an early intermediate of the aerobic benzoate pathway. The compound was with the protein but not with cell could be to compounds in containing cell extracts and a of (Fig. The conversion of benzoyl-CoA into is a reaction ring and A mechanism of benzoyl-CoA (compound 8) conversion into compound is shown in A of benzoyl-CoA (compound 8) could yield the compound of compound could compound and the of compound could be converted into or by of the or by a of or could then yield A of benzoyl-CoA (compound8) by ring in compound via compounds (Fig. However, the of to compound is under the assay conditions. a pathway via compound The benzoyl-CoA is under an catalyzing the and of has been from A. E. A. and G. to of various is to a that is by benzoate. to of suggest that a is in benzoyl-CoA in A. However, up to were not able to the of (compound could (compound which be into the 3,6-lactone of Alternatively, could to the compound which could be into the could then yield a known intermediate of the pathway. be into succinyl-CoA and acetyl-CoA (Fig. 1). The corresponding was to the and and G. The of product formation (Fig. is in with the proposed 4 (compound as an early The formation of compound be explained via product (compound which was identified in with 1 and and product 2 (compound of with an of be that the proposed reaction at the of it to be established the novel pathway is in Bacillus and in the which been to benzoate via gentisate (2Clark J.S. Buswell J.A. J. Gen. Microbiol. 1979; 112: 191-195Crossref Scopus (17) Google Scholar, 3Clark J.S. Buswell J.A. J. Gen. Microbiol. 1976; 96: 209-213Crossref PubMed Scopus (21) Google Scholar, 4Crawford R.L. J. Bacteriol. 1976; 127: 204-210Crossref PubMed Google Scholar, W. P. 3: PubMed Scopus Google Scholar). the of the proposed pathway. be that aromatic substrates as and be converted by to benzoyl-CoA benzoate. it was that containing an or of carbon be through to either benzoyl-CoA or which could be to the intermediates of metabolism E. R. B. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar). for facultative bacteria could be that which is a intermediate of the aromatic be as substrate of the aerobic metabolism when This a from the to of growth and thioester formation an of aromatic the as in the of in ligase is in the cell but is to as a protein in and for D. Scholar). The thioester is in the of the the energy initially is not for the but at the for the of the that benzoate-CoA ligase could to was that Pseudomonas the to up when the for the enzyme of a pathway of catabolism of was E. R. B. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar). is that U. Oswald B. Fuchs G. J. Bacteriol. PubMed Google Scholar, K. R. J. Fuchs G. Arch. Microbiol. Scopus Google Scholar) and J. Bacteriol. PubMed Scopus Google Scholar, H. A. J. Biol. Chem. Full Text PDF PubMed Google Scholar, S. Microbiol. 1993; PubMed Scopus Google Scholar) are aerobically in A. evansii U. Oswald B. Fuchs G. J. Bacteriol. 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