The molybdenum cofactor sulfurase ABA3 from Arabidopsis thaliana is needed for post-translational activation of aldehyde oxidase and xanthine dehydrogenase by transferring a sulfur atom to the desulfo-molybdenum cofactor of these enzymes. ABA3 is a two-domain protein consisting of an NH2-terminal NifS-like cysteine desulfurase domain and a C-terminal domain of yet undescribed function. The NH2-terminal domain of ABA3 decomposes l-cysteine to yield elemental sulfur, which subsequently is bound as persulfide to a conserved protein cysteinyl residue within this domain. In vivo, activation of aldehyde oxidase and xanthine dehydrogenase also depends on the function of the C-terminal domain, as can be concluded from the A. thaliana aba3/sir3-3 mutant. sir3-3 plants are strongly reduced in aldehyde oxidase and xanthine dehydrogenase activities due to a substitution of arginine 723 by a lysine within the C-terminal domain of the ABA3 protein. Here we present first evidence for the function of the C-terminal domain and show that molybdenum cofactor is bound to this domain with high affinity. Furthermore, cyanide-treated ABA3 C terminus was shown to release thiocyanate, indicating that the molybdenum cofactor bound to the C-terminal domain is present in the sulfurated form. Co-incubation of partially active aldehyde oxidase and xanthine dehydrogenase with ABA3 C terminus carrying sulfurated molybdenum cofactor resulted in stimulation of aldehyde oxidase and xanthine dehydrogenase activity. The data of this work suggest that the C-terminal domain of ABA3 might act as a scaffold protein where prebound desulfo-molybdenum cofactor is converted into sulfurated cofactor prior to activation of aldehyde oxidase and xanthine dehydrogenase. The molybdenum cofactor sulfurase ABA3 from Arabidopsis thaliana is needed for post-translational activation of aldehyde oxidase and xanthine dehydrogenase by transferring a sulfur atom to the desulfo-molybdenum cofactor of these enzymes. ABA3 is a two-domain protein consisting of an NH2-terminal NifS-like cysteine desulfurase domain and a C-terminal domain of yet undescribed function. The NH2-terminal domain of ABA3 decomposes l-cysteine to yield elemental sulfur, which subsequently is bound as persulfide to a conserved protein cysteinyl residue within this domain. In vivo, activation of aldehyde oxidase and xanthine dehydrogenase also depends on the function of the C-terminal domain, as can be concluded from the A. thaliana aba3/sir3-3 mutant. sir3-3 plants are strongly reduced in aldehyde oxidase and xanthine dehydrogenase activities due to a substitution of arginine 723 by a lysine within the C-terminal domain of the ABA3 protein. Here we present first evidence for the function of the C-terminal domain and show that molybdenum cofactor is bound to this domain with high affinity. Furthermore, cyanide-treated ABA3 C terminus was shown to release thiocyanate, indicating that the molybdenum cofactor bound to the C-terminal domain is present in the sulfurated form. Co-incubation of partially active aldehyde oxidase and xanthine dehydrogenase with ABA3 C terminus carrying sulfurated molybdenum cofactor resulted in stimulation of aldehyde oxidase and xanthine dehydrogenase activity. The data of this work suggest that the C-terminal domain of ABA3 might act as a scaffold protein where prebound desulfo-molybdenum cofactor is converted into sulfurated cofactor prior to activation of aldehyde oxidase and xanthine dehydrogenase. Molybdenum enzymes catalyze diverse redox reactions in the global carbon, nitrogen, and sulfur cycles (1Hille R. Chem. Rev. 1996; 96: 2757-2816Crossref PubMed Scopus (1460) Google Scholar). In all eukaryotic molybdenum enzymes, the molybdenum atom is coordinated by the dithiolene group of molybdopterin, thus forming the molybdenum cofactor (Moco) 2The abbreviations used are:Mocomolybdenum cofactorABA3-CTC-terminal domain of the Moco sulfurase ABA3 from A. thalianaAOaldehyde oxidaseICP-MSinductively plasma-coupled mass spectrometryMPTmolybdopterinXDHxanthine dehydrogenaseHPLChigh pressure liquid chromatography.2The abbreviations used are:Mocomolybdenum cofactorABA3-CTC-terminal domain of the Moco sulfurase ABA3 from A. thalianaAOaldehyde oxidaseICP-MSinductively plasma-coupled mass spectrometryMPTmolybdopterinXDHxanthine dehydrogenaseHPLChigh pressure liquid chromatography. (2Kisker C. Schindelin H. Rees D.C. Annu. Rev. Biochem. 1997; 66: 233-267Crossref PubMed Scopus (434) Google Scholar). According to the coordination chemistry of the molybdenum ligand, eukaryotic molybdenum enzymes can be divided into two groups; Moco with two additional oxo-ligands and a protein-derived cysteinyl sulfur is bound by enzymes of the sulfite oxidase family, whereas enzymes of the xanthine oxidase family have one oxygen, one inorganic sulfur, and one hydroxyl group ligated to the pterin-chelated molybdenum of the active enzyme. Among the four different molybdenum enzymes known in higher plants, sulfite oxidase and nitrate reductase belong to the sulfite oxidase family, whereas aldehyde oxidase (AO) and xanthine dehydrogenase (XDH) are members of the xanthine oxidase family (3Schwarz G. Mendel R.R. Annu. Rev. Plant Biol. 2006; 57: 623-647Crossref PubMed Scopus (246) Google Scholar). Although it is believed that all of these molybdenum enzymes basically incorporate the same type of Moco, only AO and XDH, but not enzymes of the sulfite oxidase family, require a final enzyme-dependent post-translational modification of the molybdenum center for activity (4Wahl R.C. Warner C.K. Finnerty V. Rajagopalan K.V. J. Biol. Chem. 1982; 257: 3958-3962Abstract Full Text PDF PubMed Google Scholar). During this modification step, an oxo-ligand of the Moco in inactive AO and XDH enzymes is substituted by a sulfur atom in order to activate AO and XDH. molybdenum cofactor C-terminal domain of the Moco sulfurase ABA3 from A. thaliana aldehyde oxidase inductively plasma-coupled mass spectrometry molybdopterin xanthine dehydrogenase high pressure liquid chromatography. molybdenum cofactor C-terminal domain of the Moco sulfurase ABA3 from A. thaliana aldehyde oxidase inductively plasma-coupled mass spectrometry molybdopterin xanthine dehydrogenase high pressure liquid chromatography. The first insight into the mechanism of Moco sulfuration was obtained by cloning and biochemical characterization of the Moco sulfurase protein ABA3 from Arabidopsis thaliana (5Bittner F. Oreb M. Mendel R.R. J. Biol. Chem. 2001; 276: 40381-40384Abstract Full Text Full Text PDF PubMed Scopus (240) Google Scholar, 6Heidenreich T. Wollers S. Mendel R.R. Bittner F. J. Biol. Chem. 2005; 280: 4213-4218Abstract Full Text Full Text PDF PubMed Scopus (71) Google Scholar). The NH2-terminal domain of ABA3 (ABA3-NifS) shares significant similarities to NifS-like cysteine desulfurases, whereas the C-terminal domain did not exhibit striking similarities to any other protein, except other Moco sulfurases and the recently identified mitochondrial amidoxime-reducing component (7Havemeyer A. Bittner F. Wollers S. Kunze T. Mendel R.R. Clement B. J. Biol. Chem. 2006; 281: 34796-34802Abstract Full Text Full Text PDF PubMed Scopus (124) Google Scholar). It was shown that, as typical for NifS-like enzymes, ABA3-NifS binds a pyridoxal phosphate cofactor that is essential for activity (6Heidenreich T. Wollers S. Mendel R.R. Bittner F. J. Biol. Chem. 2005; 280: 4213-4218Abstract Full Text Full Text PDF PubMed Scopus (71) Google Scholar). Furthermore, l-cysteine and l-selenocysteine are decomposed by ABA3-NifS, with l-cysteine representing the preferred substrate with a Km value 4 times lower than that for the selenium substrate. During the decomposition of l-cysteine, l-alanine is released, and elemental sulfur is generated. The sulfur is immediately coupled to a conserved cysteine residue of ABA3-NifS, thus forming a protein-bound persulfide. Co-incubation of purified ABA3-NifS and cyanide-inactivated AOα from A. thaliana as target enzyme in the presence of l-cysteine resulted in activation of the AOα protein, indicating that the persulfide sulfur was transferred from the NifS-like domain of ABA3 to the Moco of AOα. In vitro, the presence of the C-terminal domain is not required for sulfuration of xanthine oxidase family enzymes; however, there is strong evidence that it is needed in vivo. The tomato flacca mutant with a mutation in the Moco sulfurase C-terminal domain (8Sagi M. Scazzocchio C. Fluhr R. Plant J. 2002; 31: 305-317Crossref PubMed Scopus (89) Google Scholar) is strongly reduced in root AO and XDH activities and does not reveal any activities in the shoots (9Sagi M. Fluhr R. Lips S.H. Plant Physiol. 1999; 120: 571-578Crossref PubMed Scopus (77) Google Scholar). Very recently, the A. thaliana mutant sir3-3 was isolated by a sirtinol resistance screen, which is based on reduced AO activities (10Dai X. Hayashi K. Nozaki H. Cheng Y. Zhao Y. Proc. Natl. Acad. S. A. 2005; PubMed Scopus Google Scholar). sir3-3 was to have a mutation in the C-terminal domain of the indicating that the function of the C-terminal domain is required for activation of AO It was that the function of the C-terminal domain of Moco sulfurases is to the of the target enzymes one of the protein-bound (5Bittner F. Oreb M. Mendel R.R. J. Biol. Chem. 2001; 276: 40381-40384Abstract Full Text Full Text PDF PubMed Scopus (240) Google Scholar, J. A. Scazzocchio C. Finnerty V. PubMed Scopus Google Scholar). the of the C-terminal domain as sulfur Moco sulfuration (8Sagi M. Scazzocchio C. Fluhr R. Plant J. 2002; 31: 305-317Crossref PubMed Scopus (89) Google Scholar, V. 2002; Google Scholar). In this we the biochemical and characterization of the C-terminal domain of the Moco sulfurase ABA3 from A. the protein for bound that might be transferred to the ABA3 target enzymes AO and XDH. the of the sir3-3 mutation was in plants as as on the of the protein. we a for Moco of the C-terminal domain of ABA3 was into as (6Heidenreich T. Wollers S. Mendel R.R. Bittner F. J. Biol. Chem. 2005; 280: 4213-4218Abstract Full Text Full Text PDF PubMed Scopus (71) Google Scholar). The was into by and the was into the of in an NH2-terminal of and of and from A. of and was in T. C. G. 1996; PubMed Scopus Google Scholar). in in the presence of to an with and the of for a in and V. J. 1982; PubMed Google Scholar) was but in the of of AOα by T. and in the was as in H. S. M. T. T. J. Biochem. PubMed Scopus Google and C. R. Mendel R.R. Bittner F. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar, by and was by a pressure by for protein was purified on a 4 to the and in on AOα and and by from the mutant as in A. A. J. Proc. Natl. Acad. S. A. PubMed Scopus Google and in in and in the presence of reduced and where The was in a of was for the of and for reductase activity was as in A. A. J. Proc. Natl. Acad. S. A. PubMed Scopus Google of Moco and and molybdopterin and by to the to Rajagopalan K.V. Proc. Natl. Acad. S. A. 1982; PubMed Scopus Google and as in in G. Mendel R.R. J. Biol. Chem. 1997; Full Text Full Text PDF PubMed Scopus Google was by with a isolated from xanthine oxidase for which the was Rajagopalan K.V. Proc. Natl. Acad. S. A. 1982; PubMed Scopus Google Scholar). was 4 in of and activities of AO and XDH in by activity as in T. M. Plant Physiol. 1996; PubMed Scopus Google for AO and in C. R. Mendel R.R. Bittner F. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google for XDH. In of AOα and by was in a of of of AOα of with and of for by and activity with as substrate for AOα as substrate for to H. S. M. T. T. J. Biochem. PubMed Scopus Google and C. R. Mendel R.R. Bittner F. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google The of the activity by from the of on the AOα and from and to a from and a was used to by the of of protein by of to Biochem. PubMed Scopus Google of was in an of the molybdenum a and was The in by with a of and in to and The of was for by to was The was with as a and with as a The was to V. The of was with an of and a of The was The was by a a of The was for the molybdenum and with in by a to The are and an was used of that is from that be bound to the cysteinyl of and the protein was with 4 was by on a in of with of was from the protein with a and of nitrate of and of to of the The was a of Moco to a Moco protein of was it was shown to Moco and not K. A. M. J. A. Mendel R.R. G. J. Biol. Chem. 2006; 281: Full Text Full Text PDF PubMed Scopus Google Scholar). was as in K. A. M. J. A. Mendel R.R. G. J. Biol. Chem. 2006; 281: Full Text Full Text PDF PubMed Scopus Google The purified protein was for and the was used as a for was 4 for with in V. J. 1982; PubMed Google Scholar) in a protein. was from by with a The was converted to the and as The of bound to and the of to the of and and the known of The value was to the of one and based on the that the of be and bound in with and that the of be and bound in with the of was the of was the was used for of the of by on by was with of protein in of 4 two of the and was for as Plant thaliana and mutant plants and sir3-3 in in an Arabidopsis and for 4 of Plant of AO and XDH activities in was to S.H. M. Plant Physiol. 1997; PubMed Scopus Google of was 4 in of and and was to of the to a final of the in of and on of the as as of and by and with and a to the to final of The was for and on protein of protein of to and for AO and XDH activity as and of was in a protein with a mass of the is by high of the eukaryotic of Moco, purified was for to Moco In the of Moco and be identified on in was also was in the and the was reduced to of that of the protein from not of bound to in a of Moco on was for active Moco by of the is based on the of Moco from an to the nitrate reductase of the of nitrate reductase activity is H. S. M. T. T. J. Biochem. PubMed Scopus Google Scholar). from the only active Moco and not can be only Moco is of reductase activity. In the presence of however, is converted to Moco, of reductase activity as as purified in a reductase activity of in the of whereas in the presence of a activity of was Although the of bound is by these that than of the cofactor bound to is by Moco, which was to reductase activity in the molybdenum of by of the to molybdenum the in the presence of The same protein an of indicating that of the bound to molybdenum and thus from these it was not the Moco bound to is present in the which is required by the Moco sulfurase target enzymes AO and XDH, was with this sulfur is as thiocyanate, which the of nitrate an that can be by was in a of of indicating that of the sulfur ligated to of these data based on that than of the is present as Moco, and of the Moco an additional sulfur ligand, as required by enzymes of the xanthine oxidase was in the of as as molybdenum and was indicating that molybdenum in Moco on and the sulfur as from The is by the that in the did not release not of to of Moco by was different the as the of was of protein was the 4 the was to with than The final of to Moco, to reductase activity in of the mutant in the and presence of additional not data suggest that from and by In order to a for the of to purified in was with different of from C. which can be purified in and which binds Moco than the transferred to a and cofactor was from cofactor by within the was immediately converted to the and by a the same was with in the of of in the of in the presence and of of a value for cofactor to was The of bound to and the of to the of and and the known of The of the was to be a to of value of was high of to is of of and and also and the protein was Very to also the purified protein and and in to the purified protein, the of purified protein was to the and in for the of and purified protein the same and and indicating that Moco bound to is to with the and The of and to for did not significant in the and was in the presence of in with also other and was with the and that for protein was not only the redox of this but also that is obtained in a reduced purified and in a partially reduced purified It is that the sulfur of the Moco on the of the protein the of which is known to release the sulfur from the Moco of xanthine oxidase family enzymes did not of the of with in was prior to of of The of the of is by the and the of the of is by the of are by to T. G. H. C. T. J. B. R. Mendel R.R. J. Biol. Chem. 2001; 276: Full Text Full Text PDF PubMed Scopus Google Scholar) and sulfite oxidase Rajagopalan K.V. J. Biol. Chem. 1996; Full Text Full Text PDF PubMed Scopus Google Scholar) and to the recently Moco protein from C. K. A. M. J. A. Mendel R.R. G. J. Biol. Chem. 2006; 281: Full Text Full Text PDF PubMed Scopus Google the is to from the group of bound to a Rajagopalan K.V. J. Biol. Chem. 1996; Full Text Full Text PDF PubMed Scopus Google Scholar) for the domain of sulfite and we that the of and also is by a is by the that obtained from which and is to Moco, in this In on the indicating that the of this is to the it from the in the is any of the for not for and also for from C. K. A. M. J. A. Mendel R.R. G. J. Biol. Chem. 2006; 281: Full Text Full Text PDF PubMed Scopus Google Scholar). this is also in the protein in it is to the molybdenum center the and The of in Moco a mutant from A. was isolated by a based on the resistance of the mutant sirtinol (10Dai X. Hayashi K. Nozaki H. Cheng Y. Zhao Y. Proc. Natl. Acad. S. A. 2005; PubMed Scopus Google Scholar). The sir3-3 mutant was to a within the that an from arginine to lysine 723 within the C-terminal domain of the ABA3 protein. it was and to the mutation the function of the activities of target enzymes AO and XDH in of sir3-3 plants and with AO and XDH activities of other mutant plants, and Although a substitution of by within the NifS-like domain of the and are by within the by and of the (5Bittner F. Oreb M. Mendel R.R. J. Biol. Chem. 2001; 276: 40381-40384Abstract Full Text Full Text PDF PubMed Scopus (240) Google Scholar). In to of and where AO and XDH activities have of sir3-3 plants a XDH indicating that the sir3-3 mutation is to a In order to the of the sulfur is the of AO and XDH in the sir3-3 as was shown for the and S.H. M. Plant Physiol. 1997; PubMed Scopus Google of all with and this the sulfur of the Moco in AO and XDH is the activities of AO and XDH in all mutant indicating that, in and plants, the sulfuration of the Moco of AO and XDH is also in the sir3-3 mutant. the mutation into it was that the protein bound to the protein significant of a strong of also for the that the of sulfur is reduced and that not of the Moco bound to this protein is present in the and sulfur of the to the the obtained this did not to the the obtained this did not in a of AOα and by NifS-like domain of ABA3 was shown to be of AOα in vitro, whereas did not show a on the activity of AOα (6Heidenreich T. Wollers S. Mendel R.R. Bittner F. J. Biol. Chem. 2005; 280: 4213-4218Abstract Full Text Full Text PDF PubMed Scopus (71) Google Scholar). the protein used for was different and did not In the present AOα and as purified in with for prior to of AO and XDH In the activity of AOα and indicating a function of which to the activation of inactive of AOα and and The of a activity the of a in the presence of and consisting of and target enzymes AOα and In order to this the activity was from the and to an additional that this in and AOα in with ABA3 and C. R. Mendel R.R. Bittner F. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar). In of ABA3-NifS with AOα did not in of a (6Heidenreich T. Wollers S. Mendel R.R. Bittner F. J. Biol. Chem. 2005; 280: 4213-4218Abstract Full Text Full Text PDF PubMed Scopus (71) Google indicating that the C-terminal domain of ABA3 than the NifS-like domain with the target enzymes of was to also in the lower activity with AOα which the of a for activation of AOα. The of Moco sulfuration in as required by molybdenum enzymes of the xanthine oxidase family, depends on the function of Moco sulfurase enzymes. eukaryotic Moco sulfurases known to two (5Bittner F. Oreb M. Mendel R.R. J. Biol. Chem. 2001; 276: 40381-40384Abstract Full Text Full Text PDF PubMed Scopus (240) Google Scholar, M. Scazzocchio C. Fluhr R. Plant J. 2002; 31: 305-317Crossref PubMed Scopus (89) Google Scholar, J. A. Scazzocchio C. Finnerty V. PubMed Scopus Google Scholar, K. T. R. T. T. Biochem. 2001; PubMed Scopus Google Scholar, T. T. T. Y. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar, H. K. Y. H. Biochem. Biol. PubMed Scopus Google of which only the NH2-terminal NifS-like domain is basically it was shown to be for the of sulfur from l-cysteine (6Heidenreich T. Wollers S. Mendel R.R. Bittner F. J. Biol. Chem. 2005; 280: 4213-4218Abstract Full Text Full Text PDF PubMed Scopus (71) Google Scholar). Furthermore, in ABA3-NifS was shown to be to the Moco of AOα (6Heidenreich T. Wollers S. Mendel R.R. Bittner F. J. Biol. Chem. 2005; 280: 4213-4218Abstract Full Text Full Text PDF PubMed Scopus (71) Google Scholar). it was known that in the NifS-like domain also the C-terminal domain of Moco sulfurases is required for activation of AO and XDH. the Moco sulfurase mutant flacca of a within the C-terminal domain was to be the of AO and XDH (8Sagi M. Scazzocchio C. Fluhr R. Plant J. 2002; 31: 305-317Crossref PubMed Scopus (89) Google Scholar). the mutant sir3-3 from A. thaliana to be in it an to the sirtinol to which (10Dai X. Hayashi K. Nozaki H. Cheng Y. Zhao Y. Proc. Natl. Acad. S. A. 2005; PubMed Scopus Google Scholar). mutant a mutation within the C terminus of to a substitution of the conserved arginine 723 of the ABA3 protein by a lysine a type was as carrying the same mutation in the C-terminal domain of the Moco sulfurase H. A. H. PubMed Scopus Google except that the conserved arginine is for a cysteine residue not only the of the C-terminal domain for Moco sulfuration in but also the of the the conserved arginine residue 723 in ABA3 in the of the C-terminal domain for activation of AO and XDH was not as It was that the C-terminal domain might have a in the target enzymes of Moco as a to sulfur from the NifS-like domain to the Moco of AO and XDH (5Bittner F. Oreb M. Mendel R.R. J. Biol. Chem. 2001; 276: 40381-40384Abstract Full Text Full Text PDF PubMed Scopus (240) Google Scholar, J. A. Scazzocchio C. Finnerty V. PubMed Scopus Google Scholar). The of an cysteine residue within the C-terminal domain in which is also conserved in of to that the C-terminal domain might be a sulfur domain that sulfur by the NifS-like domain in the of a persulfide on conserved cysteine and it for the of sulfurated Moco V. 2002; Google Scholar). persulfide shown on the C-terminal domain of a Moco sulfurase protein to The present work evidence that the C-terminal domain of ABA3 as the scaffold for of sulfurated Moco and that of sulfurated Moco to the C-terminal domain is a for activation of AO and XDH. In to is as by the of on as a high of of which is to for the of the Moco protein with of and G. Mendel R.R. J. Biol. Chem. 1997; Full Text Full Text PDF PubMed Scopus Google the of to a of M. M. S. J. Biol. Chem. 2006; 281: Full Text Full Text PDF PubMed Scopus Google also from to It is a of and that the Moco by bound by to be on to the of molybdenum enzymes for into the Although the of Moco are not identified as it is known that are required for the of sulfurated Moco into M. PubMed Scopus Google Scholar, M. M. S. J. Biol. Chem. 2006; 281: Full Text Full Text PDF PubMed Scopus Google Scholar, S. J. 1999; PubMed Google Scholar, F. M. J. Biochem. PubMed Scopus Google which was shown to on an and the of XDH M. M. S. J. Biol. Chem. 2006; 281: Full Text Full Text PDF PubMed Scopus Google Scholar). Although of sulfurated Moco and the to with target enzymes, function is different from the function of the activity of for activation of AO and XDH is required than as in of for this obtained by the characterization of the A. thaliana which of AO and XDH the activities of enzymes in of sir3-3 plants by it was that Moco is present in enzymes but in have to that the C-terminal domain of ABA3 is not required for the of Moco into the of AO and XDH but for the post-translational sulfuration of the mutation was shown to than to and the of sulfur bound to the Moco of the to be the It that the of Moco sulfurase activity in the sir3-3 is due to the of Moco, of Moco be for significant Moco sulfurase activity for activation of AO and XDH this Moco is sulfurated that bound to is sulfurated one can that the of by than and the of sulfur are by the reduced of the protein to sulfurated that the of AO and XDH in the sir3-3 mutant is the to sulfurated Moco, and also suggest that arginine 723 is in of the sulfurated Furthermore, the obtained from the to that the C-terminal domain of ABA3 two different of Moco one with a sulfur and this additional The by which and the sulfur are in the might that only the for sulfurated Moco is whereas the for The NifS-like domain of ABA3 sulfur from l-cysteine and binds it in the of a persulfide (6Heidenreich T. Wollers S. Mendel R.R. Bittner F. J. Biol. Chem. 2005; 280: 4213-4218Abstract Full Text Full Text PDF PubMed Scopus (71) Google Scholar). It was that in the NifS-like domain of ABA3 persulfide to the conserved cysteine to persulfide the C-terminal domain, which subsequently is transferred to the Moco of AO and XDH V. 2002; Google Scholar). different from this suggest that a persulfide is bound to the C-terminal domain of this persulfide sulfur is subsequently ligated to the molybdenum atom of the Moco bound to the C-terminal domain of ABA3 than to the Moco of AO and XDH. of the of the sulfur is transferred from the C-terminal domain to AO and XDH. can be the sulfur of the Moco bound to the C-terminal domain of ABA3 is transferred as to the Moco of AO and XDH, the sulfurated Moco is transferred from the C-terminal domain of ABA3 to AO and XDH. AO and XDH by the of this by the sulfurated Moco of The that is to AOα and one of it that the C-terminal domain is of transferring sulfur to AO and XDH in a in the higher as sulfurated for the of and of for also G. for of the with
No takes yet. Share an insight, caveat, or question.
Wollers et al. (2008) studied this question.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: