An X-ray diffraction and X-ray absorption spectroscopy joint study of neuroglobin

Arcovito, Alessandro; Moschetti, Tommaso; D’Angelo, P.; Mancini, Giordano; Vallone, B.; Brunori, Maurizio; Longa, Stefano Della

doi:10.1016/j.abb.2008.03.026

Cited by 53 publications

(71 citation statements)

References 50 publications

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“…Although the resting state of the enzyme contains iron (III), it is known that prolonged X-ray exposure can cause photoreduction to iron (II) [25][26][27], which could bind dioxygen as a ligand, hence we interpret the diatomic ligand as an iron (II)-dioxygen or iron (III)-superoxide species. …”

Section: Crystal Structure Determinationmentioning

confidence: 99%

Structure of Thermobifida fusca DyP-type peroxidase and activity towards Kraft lignin and lignin model compounds

Rahmanpour

Rea

Jamshidi

et al. 2016

Archives of Biochemistry and Biophysics

102

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A Dyp-type peroxidase enzyme from thermophilic cellulose degrader Thermobifida fusca (TfuDyP) was investigated for catalytic ability towards lignin oxidation. TfuDyP was characterised kinetically against a range of phenolic substrates, and a compound I reaction intermediate was observed via pre-steady state kinetic analysis at max 404 nm. TfuDyP showed reactivity towards Kraft lignin, and was found to oxidise a -aryl ether lignin model compound, forming an oxidised dimer. A crystal structure of TfuDyP was determined, to 1.8Å resolution, which was found to contain a diatomic oxygen ligand bound to the heme centre, positioned close to active site residues Asp-203 and Arg-315. The structure contains two channels providing access to the heme cofactor for organic substrates and hydrogen peroxide. Site-directed mutant D203A showed no activity towards phenolic substrates, but reduced activity towards ABTS, while mutant R315Q showed no activity towards phenolic substrates, nor ABTS.

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Section: Crystal Structure Determinationmentioning

confidence: 99%

Structure of Thermobifida fusca DyP-type peroxidase and activity towards Kraft lignin and lignin model compounds

Rahmanpour

Rea

Jamshidi

et al. 2016

Archives of Biochemistry and Biophysics

102

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“…8 method section), and it is well known that prolonged X-ray exposure determines a reduction of the iron heme disfavoring the contamination of oxidized species [11,15]. Therefore, the observed XANES changes are due to a decrease of the first-shell average distance.…”

Section: Accepted M Manuscriptmentioning

confidence: 99%

“…An accurate structural characterization has been obtained on metal ionic solutions [12], different heme models and heme containing proteins [13][14][15], showing that a combined analysis of the EXAFS and XANES regions of the spectrum is able to provide unambiguous details on the local structure in solution around the metal center.…”

Section: Accepted Manuscriptmentioning

confidence: 99%

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Unusual proximal heme pocket geometry in the deoxygenated Thermobifida fusca: A combined spectroscopic investigation

Arcovito¹,

Bonamore²,

Hazemann³

et al. 2010

Biophysical Chemistry

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The spectroscopic properties of the deoxygenated truncated hemoglobin from the actinobacterium Thermobifida fusca have been investigated by means of extended X-ray absorption fine structure (EXAFS), X-ray absorption near edge structure (XANES), and near infrared spectroscopies both at room and cryogenic temperatures. At room temperature the near infrared charge transfer band III occurs at 772 nm, a value that is unusually high for a canonical deoxygenated hemoglobin species, and can only be found as a transient species after photolysis in vertebrate hemoglobins and myoglobins or under strongly dehydrating conditions. EXAFS and XANES quantitative analyses, carried out in parallel with deoxygenated horse myoglobin, revealed an unusually short iron-histidine distance 1.90 +/- 0.03 angstrom, significantly shorter than the deoxygenated horse myoglobin distance of 2.11 +/- 0.02 angstrom. These findings provide novel structural basis for discussing the fine structural geometry of the proximal site, and eventually mapping the coordinates of the metal with respect to the pyrrole nitrogens and the proximal histidine nitrogen. (C) 2009 Elsevier B.V. All rights reserved

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“…It is the 5-coordinate structure, which gives neuroglobin its typical globin reactivity with all the normal exogenous gaseous heme ligands (6)(7)(8)(9). Atomic resolution structures have been reported for the mouse-derived protein in both the ferric and ferrous states (10), although it appears that the reported ''ferric'' structure may well in fact be the structure of the ferrous form, generated by photo reduction in the X-ray beam (11). Neuroglobin is an extremely robust protein with the holoprotein being able to withstand temperatures over 100 8C and the apoprotein pH values as low as pH 2.0 before denaturing (12,13).…”

Section: Introductionmentioning

confidence: 98%

A role for human neuroglobin in apoptosis

et al. 2010

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SummaryOver the past decade, following the discovery of the human heme protein neuroglobin, many studies have searched for evidence for this protein's mechanism of action. Much data has accrued showing that high levels of neuroglobin will protect cells from apoptotic cell death, following a wide range of challenges. Various explanations of its actions, based on measured reactivity with oxygen, nitric oxide, or free radicals, have been proposed, but none have, as yet, been substantiated in vivo. Following preliminary experiments, it was previously hypothesised that ''the central role of neuroglobin in highly metabolically active cells and retinal and brain neurons is to reset the trigger level of mitochondrial cytochrome c release necessary to commit the cells to apoptosis'' (I.U.M.B.M. Life (2008) 60, 398). In this article, we review the evidence, which has accumulated to support this hypothesised mechanism of action of neuroglobin and integrate this data, with other reported intracellular functions of neuroglobin, to suggest a plausible central role for neuroglobin in the control of apoptosis. IUBMBIUBMB Life, 62(12): 878-885, 2010

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An X-ray diffraction and X-ray absorption spectroscopy joint study of neuroglobin

Cited by 53 publications

References 50 publications

Structure of Thermobifida fusca DyP-type peroxidase and activity towards Kraft lignin and lignin model compounds

Structure of Thermobifida fusca DyP-type peroxidase and activity towards Kraft lignin and lignin model compounds

Unusual proximal heme pocket geometry in the deoxygenated Thermobifida fusca: A combined spectroscopic investigation

A role for human neuroglobin in apoptosis

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