Vanadium K-edge X-ray absorption spectrum of the VFe protein of the vanadium nitrogenase of Azotobacter chroococcum

Arber, Judith M.; Dobson, B. R.; Eady, Robert R.; Stevens, Philippe; Hasnain, S.S.; Garner, C. David; Smith, Barry E.

doi:10.1038/325372a0

Cited by 131 publications

(77 citation statements)

References 9 publications

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“…This indicates that, in the course of cofactor synthesis, the nifB gene product is required at a step common to the pathways leading to FeMo-cofactor, FeV-cofactor (1,24,31), or the cofactor presumed to be present in nitrogenase-3 (18). The FeMo-cofactor synthesis genes, nifEN, on the other hand, are required only when A. vinelandii is fixing N2 in the presence of Mo (11), since N2 fixation in the presence of V or under Mo-deficient conditions does not require the presence of these genes.…”

Section: Discussionmentioning

confidence: 99%

“…However, the product of nifQ is not absolutely required for the synthesis of active nitrogenase. Since NifQ-mutants of K. pneumoniae can grow slowly under N2-fixing conditions in the presence of 1 ,uM Na2MoO4, the reaction catalyzed by the nifQ gene product apparently proceeds spontaneously. The growth of nifQ mutant strains in the presence of greater amounts of molybdate (100 ,M) is almost indistinguishable from that of the wild-type strain (38).…”

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confidence: 99%

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Nucleotide sequence and genetic analysis of the nifB-nifQ region from Azotobacter vinelandii

1988

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Section: Discussionmentioning

confidence: 99%

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confidence: 99%

Nucleotide sequence and genetic analysis of the nifB-nifQ region from Azotobacter vinelandii

1988

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“…One other occurrence of vanadium in a biological context, besides that of V in haloperoxidases, is that in aforementioned vanadium-dependent nitrogenases [28,127]. The XANES and EXAFS at the V K-edge of the first V-containing nitrogenase from A. chroococcum resembled very much that of a VFe 3 S 4 cubane cluster [128].…”

Section: Page 17 Of 40mentioning

confidence: 99%

Vanadium haloperoxidases: From the discovery 30 years ago to X-ray crystallographic and V K-edge absorption spectroscopic studies

Leblanc

Vilter

Fournier

et al. 2015

Coordination Chemistry Reviews

128

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In the environment, vanadium-dependent haloperoxidases (VHPO) are likely to play a key role in the production of biogenic organo-halogens. These enzymes contain vanadate as a prosthetic group, and catalyze, in the presence of hydrogen peroxide, the oxidation of halide ions (Cl -, Br -or I -). They are classified according to the most electronegative halide that they can oxidize. Since the first discovery of a vanadium bromoperoxidase in the brown alga Ascophyllum nodosum thirty years ago, structural and mechanistic studies have been mainly conducted on two types of VHPO, chloro-and bromoperoxidases, and more recently on a vanadium-dependent iodoperoxidase. In this review, we highlight the main progress obtained on the structure-function relation of these proteins, based on biochemistry, crystallography and X-ray absorption spectroscopy (XAS). The comparison of 3D protein structures of the different VHPO helped identify the residues that govern the molecular mechanisms of catalysis and specificity of VHPO. Vanadium K-edge XAS gave further important insight to understand the fine changes around the vanadium cofactor during the catalytic cycle. The combination of different structural approaches, at different scales of resolution, shed new light on biological vanadium coordination in the active site, and its importance for the catalytic cycle and halide specificity of vanadium haloperoxidases. Keywords (max 6)Vanadium-dependent haloperoxidase, vanadium coordination, crystallographic structure, structural evolution, oligomeric state, X-ray absorption spectroscopy on biological vanadium

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“…Dinitrogenase 2 has been purified from A. vinelandii (24) and A. chroococcum (18) 14,000 appears to be present in dinitrogenase 2 from A. chroococcum (17,18). Dinitrogenase 2 contains Fe and V (18,24), and a FeV cofactor analogous to the FeMo cofactor has been reported for A. chroococcum (1,60). The genetic basis of the V nitrogenase from A. vinelandii is not as well understood as it is for the V nitrogenase from A. chroococcum, but extensive similarities appear to exist within the two organisms (49, 55; our unpublished results).…”

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confidence: 93%

Nucleotide sequence and mutational analysis of the structural genes (anfHDGK) for the second alternative nitrogenase from Azotobacter vinelandii

et al. 1989

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The nucleotide sequence of a region of the Azotobacter vinelandii genome exhibiting sequence similarity to nifH has been determined. The order of open reading frames within this 6.1-kilobase-pair region was found to be anfH (alternative nitrogen fixation, nifH-like gene), anfD (nifD-like gene), anfG (potentially encoding a protein similar to the product of vnfG from Azotobacter chroococcum), anfK (nifK-like gene), followed by two additional open reading frames. The 5'-flanking region of anfH contains a nif promoter similar to that found in the A. vinelandii nifHDK gene cluster. The presumed products of anfH, anfD, and anfK are similar in predicted Mr and pI to the previously described subunits of nitrogenase 3. Deletion plus insertion mutations introduced into the anfHDGK region of wild-type strain A. vinelandii CA resulted in mutant strains that were unable to grow in Mo-deficient, N-free medium but grew in the presence of 1 microM Na2MoO4 or V2O5. Introduction of the same mutations into the nifHDK deletion strain CA11 resulted in strains that grew under diazotrophic conditions only in the presence of vanadium. The lack of nitrogenase 3 subunits in these mutant strains was demonstrated through two-dimensional gel analysis of protein extracts from cells derepressed for nitrogenase under Mo and V deficiency. These results indicate that anfH, anfD, and anfK encode structural proteins for nitrogenase 3.

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Vanadium K-edge X-ray absorption spectrum of the VFe protein of the vanadium nitrogenase of Azotobacter chroococcum

Cited by 131 publications

References 9 publications

Nucleotide sequence and genetic analysis of the nifB-nifQ region from Azotobacter vinelandii

Nucleotide sequence and genetic analysis of the nifB-nifQ region from Azotobacter vinelandii

Vanadium haloperoxidases: From the discovery 30 years ago to X-ray crystallographic and V K-edge absorption spectroscopic studies

Nucleotide sequence and mutational analysis of the structural genes (anfHDGK) for the second alternative nitrogenase from Azotobacter vinelandii

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