Resonance Raman spectroscopy of Fe–S proteins and their redox properties

Todorović, Smilja; Teixeira, Miguel

doi:10.1007/s00775-018-1533-0

Cited by 44 publications

(33 citation statements)

References 84 publications

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“…cluster decreased more than two-fold, in agreement with the strong decrease of the UV/Vis absorbance in the presence of NaDT (Figure 3A). A potential [4Fe-4S] 3+ and [4Fe-4S] 1+ cluster would be equally Raman-inactive 36 ; however, whether a cluster with an alternative geometry is formed upon oxidation or reduction is unclear at this stage. Notably, washing, and mild reduction via DTT restored the Raman modes of the as-isolated sample, which proves the full restoration of the [4Fe-4S] 2+ cluster.…”

Section: The Redox Changes Of Hypcd Are Reversiblementioning

confidence: 99%

Electron Inventory of the Iron-Sulfur Scaffold Complex HypCD Essential in [NiFe]-Hydrogenase Cofactor Assembly

Stripp

Oltmanns

Müller

et al. 2021

Preprint

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The [4Fe-4S] cluster containing scaffold complex HypCD is the central construction site for the assembly of the [Fe](CN)2CO cofactor precursor of [NiFe]-hydrogenase. While the importance of the HypCD complex is well established, not much is known about the mechanism by which the CN– and CO ligands are transferred and attached to the iron ion. We developed an efficient protocol for the production and isolation of the functional HypCD complex that facilitated detailed spectroscopic investigations. The results obtained by UV/Vis-, electron paramagnetic Resonance (EPR)-, Resonance Raman-, Fourier-transform infrared (FTIR), and Mössbauer spectroscopy provide comprehensive evidence for an electron inventory fit to drive multi-electron redox reactions. We demonstrate the redox activity of the HypCD complex reporting the interconversion of the [4Fe-4S]2+/+ couple. Additionally, we observed a reversible redox conversion between the [4Fe-4S]2+ and a [3Fe-4S]+ cluster. MicroScale thermophoresis indicated preferable binding between the HypCD complex and its interaction partner HypEF under reducing conditions. Together, these results suggest a redox cascade involving the [4Fe-4S] cluster and a conserved disulﬁde bond of HypD that may facilitate the synthesis of the [Fe](CN)2CO cofactor precursor on the HypCD scaffold complex.

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Section: The Redox Changes Of Hypcd Are Reversiblementioning

confidence: 99%

Electron Inventory of the Iron-Sulfur Scaffold Complex HypCD Essential in [NiFe]-Hydrogenase Cofactor Assembly

Stripp

Oltmanns

Müller

et al. 2021

Preprint

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“…29 There are many different enzymes in the body that contain iron in the catalytic site that can be categorized in 3 major groups: iron-sulfur proteins; heme-containing proteins; and iron-proteins that are devoid of iron-sulfur clusters or heme. 49,50 Among them are Fe-dependent oxygenases, including tryptophan dioxygenase, ferredoxin, and 2-oxoglutarate dioxygenase, iron-sulfur proteins, catalase, and so on. Notably, only the enzymes of the lipoxygenases (LOX) family and heme-containing peroxidases can oxidize lipids under physiologically relevant conditions.…”

Section: Fe-proteins and Mechanism Of Enzymatic Oxidationmentioning

confidence: 99%

Redox (phospho)lipidomics of signaling in inflammation and programmed cell death

Tyurina

Croix

Watkins

et al. 2019

Journal of Leukocyte Biology

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In addition to the known prominent role of polyunsaturated (phospho)lipids as structural blocks of biomembranes, there is an emerging understanding of another important function of these molecules as a highly diversified signaling language utilized for intra-and extracellular communications. Technological developments in high-resolution mass spectrometry facilitated the development of a new branch of metabolomics, redox lipidomics. Analysis of lipid peroxidation reactions has already identified specific enzymatic mechanisms responsible for the biosynthesis of several unique signals in response to inflammation and regulated cell death programs. Obtaining comprehensive information about millions of signals encoded by oxidized phospholipids, represented by thousands of interactive reactions and pleiotropic (patho)physiological effects, is a daunting task.However, there is still reasonable hope that significant discoveries, of at least some of the important contributors to the overall overwhelmingly complex network of interactions triggered by inflammation, will lead to the discovery of new small molecule regulators and therapeutic modalities. For example, suppression of the production of AA-derived pro-inflammatory mediators, HXA 3 and LTB 4, by an iPLA 2 inhibitor, R-BEL, mitigated injury associated with the activation of pro-inflammatory processes in animals exposed to whole-body irradiation. Further, technological developments promise to make redox lipidomics a powerful approach in the arsenal of diagnostic and therapeutic instruments for personalized medicine of inflammatory diseases and conditions. K E Y W O R D Seicosanoids, lipid mediators, lipoxygenase, Oxidized phospholipids, peroxidation, phospholipase A2, phospholipid hydrolysis

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“…Different well-established experimental techniques exist for probing the various states of the catalytic cycle, as well as the physicochemical properties of FeS clusters. Among those, electron paramagnetic resonance (EPR) [10][11][12], infrared IR [13][14][15][16], resonance Raman (RR) [13][14][15][16][17], and Mössbauer [18] spectroscopy are powerful complementary techniques allowing the description of structural and electronic properties of the metal clusters [19]. EPR, based on microwave radiation, is well-suited to studying systems containing unpaired electrons, common for high-spin Fe centers [20].…”

Section: Introductionmentioning

confidence: 99%

Electronic and Structural Properties of the Double Cubane Iron-Sulfur Cluster

2021

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The double-cubane cluster (DCC) refers to an [Fe8S9] iron-sulfur complex that is otherwise only known to exist in nitrogenases. Containing a bridging µ2-S ligand, the DCC in the DCC-containing protein (DCCP) is covalently linked to the protein scaffold via six coordinating cysteine residues. In this study, the nature of spin coupling and the effect of spin states on the cluster’s geometry are investigated computationally. Using density functional theory (DFT) and a broken symmetry (BS) approach to study the electronic ground state of the system, we computed the exchange interaction between the spin-coupled spins of the four FeFe dimers contained in the DCC. This treatment yields results that are in excellent agreement with both computed and experimentally determined exchange parameters for analogously coupled di-iron complexes. Hybrid quantum mechanical (QM)/molecular mechanical (MM) geometry optimizations show that cubane cluster A closest to charged amino acid side chains (Arg312, Glu140, Lys146) is less compact than cluster B, indicating that electrons of the same spin in a charged environment seek maximum separation. Overall, this study provides the community with a fundamental reference for subsequent studies of DCCP, as well as for investigations of other [Fe8S9]-containing enzymes.

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Resonance Raman spectroscopy of Fe–S proteins and their redox properties

Cited by 44 publications

References 84 publications

Electron Inventory of the Iron-Sulfur Scaffold Complex HypCD Essential in [NiFe]-Hydrogenase Cofactor Assembly

Electron Inventory of the Iron-Sulfur Scaffold Complex HypCD Essential in [NiFe]-Hydrogenase Cofactor Assembly

Redox (phospho)lipidomics of signaling in inflammation and programmed cell death

Electronic and Structural Properties of the Double Cubane Iron-Sulfur Cluster

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