Vanadium K-edge absorption spectrum of bromoperoxidase from Ascophyllum nodosum

Hormes, J.; Kuetgens, U.; Chauvistré, R.; Schreiber, W.; Anders, Nils; Vilter, H.; Rehder, Dieter; Weidemann, Carola

doi:10.1016/0167-4838(88)90146-x

Cited by 42 publications

(17 citation statements)

References 20 publications

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“…At energies above the 1s + 4p transition, absorption features may arise from a transition to higher np states and multiple scattering. The recorded spectra display a substantially higher resolution than earlier XANES data [5,6], with features such as the shakedown transition not seen before. The high-resolution X-ray absorption spectra allow a detailed comparison with vanadium model compounds and discussion of the coordination type of native and oxidized V-BrPO, as shown elsewhere [l 11.…”

Section: Resultsmentioning

confidence: 90%

“…However, no such interaction could be substantiated using X-ray absorption spectroscopy [5,6]. As proposed by Arber et al, low substrate concentrations (10 mM H202) might have been responsible for this observation [5].…”

Section: Resultsmentioning

confidence: 92%

“…To date, the detailed structure and role of the active site of V-BrPO is not known. Binding of hydrogen peroxide as one of the substrates (HzOz or Br-) at the 5 vanadium center has been postulated [4] but could not be detected by earlier X-ray absorption measurements [5,6]. The optimum proton concentration for the enzyme is between pH 5 and 6.5.…”

Section: Introductionmentioning

confidence: 99%

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High‐resolution XANES studies on vanadium‐containing haloperoxidase: pH‐dependence and substrate binding

et al. 1993

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High-resolution X-ray absorption vanadium K-edge spectra were recorded for samples of vanadium-containing bromoperoxidase from the brown alga, Ascophyllum nodosum, at pH 9, 7, 5 and 4, as well as for enzyme samples containing the substrates, hydrogen peroxide and bromide. The well-resolved features of the XANES spectra are discussed. The pH-dependence of the structure of the active site has been studied revealing no significant change of the absorption features. We were able to detect an interaction of HrOr with the vanadium site of the bromoperoxidase using XAS spectroscopy, whereas addition of bromide causes no energy shift of the XANES spectrum. The possible role of vanadium during the enzymatic reaction is discussed on the basis of our results.

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Section: Resultsmentioning

confidence: 90%

Section: Resultsmentioning

confidence: 92%

Section: Introductionmentioning

confidence: 99%

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High‐resolution XANES studies on vanadium‐containing haloperoxidase: pH‐dependence and substrate binding

et al. 1993

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“…Studies on the vanadium-containing haloperoxidases started with XANES of the brown alga A. nodosum bromoperoxidase [41]. The prominent pre-edge peak at 5469 eV ( Figure 5A) is ascribed to a 1s-3d transition which is dipole-forbidden and absent in octahedral VO [129] but very strong in tetrahedral vanadate ( Figure 5A).…”

Section: Early Vanadium Haloperoxidase Xanes Resultsmentioning

confidence: 99%

“…Since its discovery, AnI was used as a laboratory model enzyme for the understanding of VHPO properties. Numerous further studies were carried out to characterize the V coordination inside the active site of AnI (later called An-VBPOI in this review), based on electron paramagnetic resonance [26,34,35], on 51 V NMR [36][37][38], X-ray crystallography [39,40] and on XAS ( [41][42][43] see below).…”

Section: Ascophylum Nodosummentioning

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

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124

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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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Halogenation and Vanadium Haloperoxidases

Fournier

Leblanc

2014

Outstanding Marine Molecules

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In marine organisms, vanadium haloperoxidases (VHPO) are involved in the production of halogenated metabolites, which feature a large panel of biological roles, such as signal molecules or antibiotics. VHPO-based halogenation processes are likely to play a role in the biogeochemical cycling of halogens because of the formation of volatile halocarbons, especially in marine coastal environments where large seaweed beds dominate. At the biochemical level, these enzymes present different specificities, and are classified according to the most electronegative halide that they can oxidize. In this chapter, a review is provided of all data obtained from biochemical, molecular characterization and structural studies on these haloperoxidases, since their discovery in a marine brown alga 30 years ago.

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Vanadium K-edge absorption spectrum of bromoperoxidase from Ascophyllum nodosum

Cited by 42 publications

References 20 publications

High‐resolution XANES studies on vanadium‐containing haloperoxidase: pH‐dependence and substrate binding

High‐resolution XANES studies on vanadium‐containing haloperoxidase: pH‐dependence and substrate binding

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

Halogenation and Vanadium Haloperoxidases

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