@article {69846, title = {Far-red fluorescent genetically encoded calcium ion indicators.}, journal = {Nat Commun}, volume = {16}, year = {2025}, month = {2025 Apr 07}, pages = {3318}, abstract = {

Genetically encoded calcium ion (Ca) indicators (GECIs) are widely-used molecular tools for functional imaging of Ca dynamics and neuronal activities with single-cell resolution. Here we report the design and development of two far-red fluorescent GECIs, FR-GECO1a and FR-GECO1c, based on the monomeric far-red fluorescent proteins mKelly1 and mKelly2. FR-GECOs have excitation and emission maxima at ~596 nm and ~644 nm, respectively, display large responses to Ca in vitro (ΔF/F = 6 for FR-GECO1a, 18 for FR-GECO1c), are bright under both one-photon and two-photon illumination, and have high affinities (apparent K = 29 nM for FR-GECO1a, 83 nM for FR-GECO1c) for Ca. FR-GECOs offer sensitive and fast detection of single action potentials in neurons, and enable in vivo all-optical manipulation and measurement of cellular activities in combination with optogenetic actuators.

Preprint:\ https://doi.org/10.1101/2020.11.12.380089

}, keywords = {Action Potentials, Animals, Calcium, Fluorescent Dyes, HEK293 Cells, Humans, Luminescent Proteins, Mice, Neurons, Optogenetics, Red Fluorescent Protein}, issn = {2041-1723}, doi = {10.1038/s41467-025-58485-z}, url = {https://doi.org/10.1038/s41467-025-58485-z}, author = {Dalangin, Rochelin and Jia, Bill Z and Qi, Yitong and Aggarwal, Abhi and Sakoi, Kenryo and Drobizhev, Mikhail and Molina, Rosana S and Patel, Ronak and Abdelfattah, Ahmed S and Zheng, Jihong and Reep, Daniel and Hasseman, Jeremy P and Zhao, Yufeng and Wu, Jiahui and Podgorski, Kaspar and Tebo, Alison G and Schreiter, Eric R and Hughes, Thomas E and Terai, Takuya and Paquet, Marie-Eve and Megason, Sean G and Cohen, Adam E and Shen, Yi and Campbell, Robert E} } @article {68836, title = {Method To Diversify Cyanine Chromophore Functionality Enables Improved Biomolecule Tracking and Intracellular Imaging.}, journal = {Journal of the American Chemical Society}, volume = {145}, year = {2023}, month = {2023 Jun 27}, pages = {14647{\textendash}14659}, abstract = {

Heptamethine indocyanines are invaluable probes for near-infrared (NIR) imaging. Despite broad use, there are only a few synthetic methods to assemble these molecules, and each has significant limitations. Here, we report the use of pyridinium benzoxazole (PyBox) salts as heptamethine indocyanine precursors. This method is high yielding, simple to implement, and provides access to previously unknown chromophore functionality. We applied this method to create molecules to address two outstanding objectives in NIR fluorescence imaging. First, we used an iterative approach to develop molecules for protein-targeted tumor imaging. When compared to common NIR fluorophores, the optimized probe increases the tumor specificity of monoclonal antibody (mAb) and nanobody conjugates. Second, we developed cyclizing heptamethine indocyanines with the goal of improving cellular uptake and fluorogenic properties. By modifying both the electrophilic and nucleophilic components, we demonstrate that the solvent sensitivity of the ring-open/ring-closed equilibrium can be modified over a wide range. We then show that a chloroalkane derivative of a compound with tuned cyclization properties undergoes particularly efficient no-wash live cell imaging using organelle-targeted HaloTag self-labeling proteins. Overall, the chemistry reported here broadens the scope of accessible chromophore functionality, and, in turn, enables the discovery of NIR probes with promising properties for advanced imaging applications.

}, issn = {1520-5126}, doi = {10.1021/jacs.3c01765}, author = {Usama, Syed Muhammad and Marker, Sierra C and Li, Dong-Hao and Caldwell, Donald R and Stroet, Marcus and Patel, Nimit L and Tebo, Alison G and Hernot, Sophie and Kalen, Joseph D and Schnermann, Martin} } @article {68770, title = {The power of peer networking for improving STEM faculty job applications: a successful pilot programme.}, journal = {Proceedings. Biological Sciences}, volume = {290}, year = {2023}, month = {2023 Apr 26}, pages = {20230124}, abstract = {

To attain a faculty position, postdoctoral fellows submit job applications that require considerable time and effort to produce. Although mentors and colleagues review these applications, postdocs rarely receive iterative feedback from reviewers with the breadth of expertise typically found on an academic search committee. To address this gap, we describe an international peer-reviewing programme for postdocs across disciplines to receive reciprocal, iterative feedback on faculty applications. A participant survey revealed that nearly all participants would recommend the programme to others. Furthermore, our programme was more likely to attract postdocs who struggled to find mentoring, possibly because of their identity as a woman or member of an underrepresented population in STEM or because they changed fields. Between 2018 and 2021, our programme provided nearly 150 early career academics with a diverse and supportive community of peer mentors during the difficult search for a faculty position and continues to do so today. As the transition from postdoc to faculty represents the largest {\textquoteright}leak{\textquoteright} in the academic pipeline, implementation of similar programmes by universities or professional societies would provide psycho-social support necessary to prevent attrition of individuals from underrepresented populations as well as increase the chances of success for early career academics in their search for independence.

}, keywords = {Faculty, Female, Humans, Mentoring, Mentors, Peer Group, Pilot Projects}, issn = {1471-2954}, doi = {10.1098/rspb.2023.0124}, author = {Guardia, Carlos M and Kane, Erin and Tebo, Alison G and Sanders, Anna A W M and Kaya, Devrim and Grogan, Kathleen E} } @article {67863, title = {Fluorescent chemigenetic actuators and indicators for use in living animals.}, journal = {Current Opinion in Pharmacology}, volume = {62}, year = {2022}, month = {2022 Jan 15}, pages = {159-167}, abstract = {

Fluorescent indicators and actuators provide a means to optically observe and perturb dynamic events in living animals. Although chemistry and protein engineering have contributed many useful tools to observe and perturb cells, an emerging strategy is to use chemigenetics: systems in which a small molecule dye interacts with a genetically encoded protein domain. Here we review chemigenetic strategies that have been successfully employed in living animals as photosensitizers for photoablation experiments, fluorescent cell cycle indicators, and fluorescent indicators for studying dynamic biological signals. Although these strategies at times suffer from challenges, e.g. delivery of the small molecule and assembly of the chemigenetic unit in living animals, the advantages of using small molecules with high brightness, low photobleaching, no chromophore maturation time and expanded color palette, combined with the ability to genetically target them to specific cell types, make chemigenetic fluorescent actuators and indicators an attractive strategy for use in living animals.

}, issn = {1471-4973}, doi = {10.1016/j.coph.2021.12.007}, author = {Farrants, Helen and Tebo, Alison G} } @article {67807, title = {Engineering of a fluorescent chemogenetic reporter with tunable color for advanced live-cell imaging.}, journal = {Nature Communications}, volume = {12}, year = {2021}, month = {2021 Nov 30}, pages = {6989}, abstract = {

Biocompatible fluorescent reporters with spectral properties spanning the entire visible spectrum are indispensable tools for imaging the biochemistry of living cells and organisms in real time. Here, we report the engineering of a fluorescent chemogenetic reporter with tunable optical and spectral properties. A collection of fluorogenic chromophores with various electronic properties enables to generate bimolecular fluorescent assemblies that cover the visible spectrum from blue to red using a single protein tag engineered and optimized by directed evolution and rational design. The ability to tune the fluorescence color and properties through simple molecular modulation provides a broad experimental versatility for imaging proteins in live cells, including neurons, and in multicellular organisms, and opens avenues for optimizing F{\"o}rster resonance energy transfer (FRET) biosensors in live cells. The ability to tune the spectral properties and fluorescence performance enables furthermore to match the specifications and requirements of advanced super-resolution imaging techniques.

}, issn = {2041-1723}, doi = {10.1038/s41467-021-27334-0}, author = {Benaissa, Hela and Ounoughi, Karim and Aujard, Isabelle and Fischer, Evelyne and Go{\"\i}ame, Rosette and Nguyen, Julie and Tebo, Alison G and Li, Chenge and Le Saux, Thomas and Bertolin, Giulia and Tramier, Marc and Danglot, Lydia and Pietrancosta, Nicolas and Morin, Xavier and Jullien, Ludovic and Gautier, Arnaud} } @article {66028, title = {Structure-Function Dataset Reveals Environment Effects within a Fluorescent Protein Model System.}, journal = {Angew Chemie (International Edition English)}, year = {2021}, month = {2021 Feb 04}, abstract = {

Anisotropic environments can drastically alter the spectroscopy and photochemistry of molecules, leading to complex structure-function relationships. We examined this using fluorescent proteins as easy-to-modify model systems. Starting from a single scaffold, we have developed a range of 27 photochromic fluorescent proteins that cover a broad range of spectroscopic properties, including the determination of 43 crystal structures. Correlation and principal component analysis confirmed the complex relationship between structure and spectroscopy, but also allowed us to identify consistent trends and to relate these to the spatial organization. We find that changes in spectroscopic properties can come about through multiple underlying mechanisms, of which polarity, hydrogen bonding and presence of water molecules are key modulators. We anticipate that our findings and rich structure/spectroscopy dataset can open opportunities for the development and evaluation of new and existing protein engineering methods.

}, issn = {1521-3773}, doi = {10.1002/anie.202015201}, author = {De Zitter, Elke and Hugelier, Siewert and Duw{\'e}, Sam and Vandenberg, Wim and Tebo, Alison G and Van Meervelt, Luc and Dedecker, Peter} } @article {67833, title = {Versatile On-Demand Fluorescent Labeling of Fusion Proteins Using Fluorescence-Activating and Absorption-Shifting Tag (FAST).}, journal = {Methods Mol Biol}, volume = {2350}, year = {2021}, month = {2021}, pages = {253-265}, abstract = {

Observing the localization, the concentration, and the distribution of proteins in cells or organisms is essential to understand theirs functions. General and versatile methods allowing multiplexed imaging of proteins under a large variety of experimental conditions are thus essential for deciphering the inner workings of cells and organisms. Here, we present a general method based on the non-covalent labeling of a small protein tag, named FAST (fluorescence-activating and absorption-shifting tag), with various fluorogenic ligands that light up upon labeling, which makes the simple, robust, and versatile on-demand labeling of fusion proteins in a wide range of experimental systems possible.

}, keywords = {Animals, Cell Line, Flow Cytometry, Fluorescent Dyes, Humans, Microscopy, Fluorescence, Molecular Structure, Recombinant Fusion Proteins, Staining and Labeling, Zebrafish}, issn = {1940-6029}, doi = {10.1007/978-1-0716-1593-5_16}, author = {Gautier, Arnaud and Jullien, Ludovic and Li, Chenge and Plamont, Marie-Aude and Tebo, Alison G and Thauvin, Marion and Volovitch, Michel and Vriz, Sophie} } @article {65763, title = {A far-red fluorescent chemogenetic reporter for in vivo molecular imaging}, journal = {Angewandte Chemie International Edition}, year = {2020}, month = {06/2020}, abstract = {

Far-red emitting fluorescent labels are highly desirable for spectral multiplexing and deep tissue imaging. Here, we describe the generation of frFAST (far-red Fluorescence Activating and absorption Shifting Tag), a 14-kDa monomeric protein that forms a bright far-red fluorescent assembly with (4-hydroxy-3-methoxy-phenyl)allylidene rhodanine (HPAR-3OM). As HPAR-3OM is essentially non- fluorescent in solution and in cells, frFAST can be imaged with high contrast in presence of free HPAR-3OM, which allowed the rapid and efficient imaging of frFAST fusions in live cells, zebrafish embryo/larvae and chicken embryo. Beyond enabling genetic encoding of far-red fluorescence, frFAST allowed the design of a far- red chemogenetic reporter of protein-protein interactions, demonstrating its great potential for the design of innovative far-red emitting biosensors.

}, issn = {1433-7851}, doi = {10.1002/anie.202006576}, author = {Li, Chenge and Tebo, Alison G and Thauvin, Marion and Plamont, Marie-Aude and Volovitch, Michel and Morin, Xavier and Vriz, Sophie and Gautier, Arnaud} } @article {65764, title = {Simple imaging protocol for autofluorescence elimination and optical sectioning in fluorescence endomicroscopy}, journal = {Optica}, volume = {6}, year = {2019}, month = {07/2019}, pages = {972}, abstract = {

Fiber-optic epifluorescence imaging with one-photon excitation benefits from its ease of use, cheap light sources, and full-frame acquisition, which enables it for favorable temporal resolution of image acquisition. However, it suffers from a lack of robustness against autofluorescence and light scattering. Moreover, it cannot easily eliminate the out-of-focus background, which generally results in low-contrast images. In order to overcome these limitations, we have implemented fast out-of-phase imaging after optical modulation (Speed OPIOM) for dynamic contrast in fluorescence endomicroscopy. Using a simple and cheap optical-fiber bundle-based endomicroscope integrating modulatable light sources, we first showed that Speed OPIOM provides intrinsic optical sectioning, which restricts the observation of fluorescent labels at targeted positions within a sample. We also demonstrated that this imaging protocol efficiently eliminates the interference of autofluorescence arising from both the fiber bundle and the specimen in several biological samples. Finally, we could perform multiplexed observations of two spectrally similar fluorophores differing by their photoswitching dynamics. Such attractive features of Speed OPIOM in fluorescence endomicroscopy should find applications in bioprocessing, clinical diagnostics, plant observation, and surface imaging.

}, doi = {10.1364/optica.6.000972}, author = {Zhang, Ruikang and Chouket, Raja and Tebo, Alison G and Plamont, Marie-Aude and Kelemen, Zsolt and Gissot, Lionel and Faure, Jean-Denis and Gautier, Arnaud and Croquette, Vincent and Jullien, Ludovic and Saux, Thomas Le} } @article {65765, title = {A split fluorescent reporter with rapid and reversible complementation.}, journal = {Nature communications}, volume = {10}, year = {2019}, month = {06/2019}, pages = {2822}, abstract = {

Interactions between proteins play an essential role in metabolic and signaling pathways, cellular processes and organismal systems. We report the development of splitFAST, a fluorescence complementation system for the visualization of transient protein-protein interactions in living cells. Engineered from the fluorogenic reporter FAST (Fluorescence-Activating and absorption-Shifting Tag), which specifically and reversibly binds fluorogenic hydroxybenzylidene rhodanine (HBR) analogs, splitFAST displays rapid and reversible complementation, allowing the real-time visualization of both the formation and the dissociation of a protein assembly.

}, doi = {10.1038/s41467-019-10855-0}, author = {Tebo, Alison G and Gautier, Arnaud} } @article {65772, title = {Circularly Permuted Fluorogenic Proteins for the Design of Modular Biosensors.}, journal = {ACS Chemical Biology}, volume = {13}, year = {2018}, month = {09/2018}, pages = {2392 {\textendash} 2397}, abstract = {

Fluorescent reporters are essential components for the design of optical biosensors that are able to image intracellular analytes in living cells. Herein, we describe the development of circularly permuted variants of Fluorescence-Activating and absorption-Shifting Tag (FAST) and demonstrate their potential as reporting module in biosensors. Circularly permutated FAST (cpFAST) variants allow one to condition the binding and activation of a fluorogenic ligand (and thus fluorescence) to analyte recognition by coupling them with analyte-binding domains. We demonstrated their use for biosensor design by generating multicolor plug-and-play fluorogenic biosensors for imaging the intracellular levels of Ca2+ in living mammalian cells in real time.

}, doi = {10.1021/acschembio.8b00417}, author = {Tebo, Alison G and Pimenta, Frederico M and Zoumpoulaki, Martha and Kikuti, Carlos and Sirkia, Helena and Plamont, Marie-Aude and Houdusse, Anne and Gautier, Arnaud} } @article {65771, title = {Development of a Rubredoxin-Type Center Embedded in a de Dovo-Designed Three-Helix Bundle}, journal = {Biochemistry}, volume = {57}, year = {2018}, month = {03/2018}, pages = {2308 {\textendash} 2316}, abstract = {

Protein design is a powerful tool for interrogating the basic requirements for the function of a metal site in a way that allows for the selective incorporation of elements that are important for function. Rubredoxins are small electron transfer proteins with a reduction potential centered near 0 mV (vs normal hydrogen electrode). All previous attempts to design a rubredoxin site have focused on incorporating the canonical CXXC motifs in addition to reproducing the peptide fold or using flexible loop regions to define the morphology of the site. We have produced a rubredoxin site in an utterly different fold, a three-helix bundle. The spectra of this construct mimic the ultraviolet{\textendash}visible, M{\"o}ssbauer, electron paramagnetic resonance, and magnetic circular dichroism spectra of native rubredoxin. Furthermore, the measured reduction potential suggests that this rubredoxin analogue could function similarly. Thus, we have shown that an α-helical scaffold sustains a rubredoxin site that can cycle with the desired potential between the Fe(II) and Fe(III) states and reproduces the spectroscopic characteristics of this electron transport protein without requiring the classic rubredoxin protein fold.

}, doi = {10.1021/acs.biochem.8b00091}, url = {https://pubs-acs-org.accesdistant.sorbonne-universite.fr/doi/pdf/10.1021/acs.biochem.8b00091}, author = {Tebo, Alison G and Pinter, Tyler B J and Garc{\'\i}a-Serres, Ricardo and Speelman, Amy L and Tard, C{\'e}dric and S{\'e}n{\`e}que, Olivier and Blondin, Genevi{\`e}ve and Latour, Jean-Marc and Penner-Hahn, James and Lehnert, Nicolai and Pecoraro, Vincent L} } @article {65769, title = {Improved Chemical-Genetic Fluorescent Markers for Live Cell Microscopy}, journal = {Biochemistry}, volume = {57}, year = {2018}, month = {11/2018}, pages = {5648 {\textendash} 5653}, abstract = {

Inducible chemical-genetic fluorescent markers are promising tools for live cell imaging requiring high spatiotemporal resolution and low background fluorescence. The fluorescence-activating and absorption shifting tag (FAST) was recently developed to form fluorescent molecular complexes with a family of small, synthetic fluorogenic chromophores (so-called fluorogens). Here, we use rational design to modify the binding pocket of the protein and screen for improved fluorescence performances with four different fluorogens. The introduction of a single mutation results in improvements in both quantum yield and dissociation constant with nearly all fluorogens tested. Our improved FAST (iFAST) allowed the generation of a tandem iFAST (td-iFAST) that forms green and red fluorescent reporters 1.6-fold and 2-fold brighter than EGFP and mCherry, respectively, while having a comparable size.

}, doi = {10.1021/acs.biochem.8b00649}, url = {https://pubs-acs-org.accesdistant.sorbonne-universite.fr/doi/pdf/10.1021/acs.biochem.8b00649}, author = {Tebo, Alison G and Pimenta, Frederico M and Zhang, Yu and Gautier, Arnaud} } @article {65768, title = {Macroscale fluorescence imaging against autofluorescence under ambient light}, journal = {Light: Science \& Applications}, year = {2018}, month = {11/2018}, pages = {1 {\textendash} 12}, abstract = {

Macroscale fluorescence imaging is increasingly used to observe biological samples. However, it may suffer from spectral interferences that originate from ambient light or autofluorescence of the sample or its support. In this manuscript, we built a simple and inexpensive fluorescence macroscope, which has been used to evaluate the performance of Speed OPIOM (Out of Phase Imaging after Optical Modulation), which is a reference-free dynamic contrast protocol, to selectively image reversibly photoswitchable fluorophores as labels against detrimental autofluorescence and ambient light. By tuning the intensity and radial frequency of the modulated illumination to the Speed OPIOM resonance and adopting a phase-sensitive detection scheme that ensures noise rejection, we enhanced the sensitivity and the signal-to-noise ratio for fluorescence detection in blot assays by factors of 50 and 10, respectively, over direct fluorescence observation under constant illumination. Then, we overcame the strong autofluorescence of growth media that are currently used in microbiology and realized multiplexed fluorescence observation of colonies of spectrally similar fluorescent bacteria with a unique configuration of excitation and emission wavelengths. Finally, we easily discriminated fluorescent labels from the autofluorescent and reflective background in labeled leaves, even under the interference of incident light at intensities that are comparable to sunlight. The proposed approach is expected to find multiple applications, from biological assays to outdoor observations, in fluorescence macroimaging.

}, doi = {10.1038/s41377-018-0098-6}, author = {Zhang, Ruikang and Chouket, Raja and Plamont, Marie-Aude and Kelemen, Zsolt and Espagne, Agathe and Tebo, Alison G and Gautier, Arnaud and Gissot, Lionel and Faure, Jean-Denis and Jullien, Ludovic and Croquette, Vincent and Saux, Thomas Le} } @article {65766, title = {Modifying the Steric Properties in the Second Coordination Sphere of Designed Peptides Leads to Enhancement of Nitrite Reductase Activity}, journal = {Angewandte Chemie International Edition}, volume = {57}, year = {2018}, month = {01/2018}, pages = {3954 {\textendash} 3957}, abstract = {

Protein design is a useful strategy to interrogate the protein structure-function relationship. We demonstrate using a highly modular 3-stranded coiled coil (TRI-peptide system) that a functional type 2 copper center exhibiting copper nitrite reductase (NiR) activity exhibits the highest homogeneous catalytic efficiency under aqueous conditions for the reduction of nitrite to NO and H2O. Modification of the amino acids in the second coordination sphere of the copper center increases the nitrite reductase activity up to 75-fold compared to previously reported systems. We find also that steric bulk can be used to enforce a three-coordinate CuI in a site, which tends toward two-coordination with decreased steric bulk. This study demonstrates the importance of the second coordination sphere environment both for controlling metal-center ligation and enhancing the catalytic efficiency of metalloenzymes and their analogues.

}, doi = {10.1002/anie.201712757}, url = {https://onlinelibrary.wiley.com/doi/full/10.1002/anie.201712757}, author = {Koebke, Karl J and Yu, Fangting and Salerno, Elvin and Stappen, Casey Van and Tebo, Alison G and Penner-Hahn, James E and Pecoraro, Vincent L} } @article {65773, title = {Intramolecular Photogeneration of a Tyrosine Radical in a Designed Protein}, journal = {ChemPhotoChem}, volume = {1}, year = {2017}, month = {02/2017}, pages = {89 {\textendash} 92}, abstract = {

Long-distance biological electron transfer occurs through a hopping mechanism and often involves tyrosine as a high potential intermediate, for example in the early charge separation steps during photosynthesis. Protein design allows for the development of minimal systems to study the underlying principles of complex systems. Herein, we report the development of the first ruthenium-linked designed protein for the photogeneration of a tyrosine radical by intramolecular electron transfer.

}, doi = {10.1002/cptc.201600044}, url = {https://chemistry-europe.onlinelibrary.wiley.com/doi/abs/10.1002/cptc.201600044}, author = {Tebo, Alison G and Quaranta, Annamaria and Herrero, Christian and Pecoraro, Vincent L and Aukauloo, Ally} } @article {65782, title = {Artificial metalloenzymes derived from three-helix bundles.}, journal = {Current Opinion in Chemical Biology}, volume = {25C}, year = {2015}, month = {01/2015}, pages = {65 {\textendash} 70}, abstract = {

Three-helix bundles and coiled-coil motifs are well-established de novo designed scaffolds that have been investigated for their metal-binding and catalytic properties. Satisfaction of the primary coordination sphere for a given metal is sufficient to introduce catalytic activity and a given structure may catalyze different reactions dependent on the identity of the incorporated metal. Here we describe recent contributions in the de novo design of metalloenzymes based on three-helix bundles and coiled-coil motifs, focusing on non-heme systems for hydrolytic and redox chemistry.

}, doi = {10.1016/j.cbpa.2014.12.034}, author = {Tebo, Alison G and Pecoraro, Vincent L} } @article {65781, title = {Variable primary coordination environments of Cd(II) binding to three helix bundles provide a pathway for rapid metal exchange.}, journal = {Metallomics}, volume = {7}, year = {2015}, month = {10/2015}, pages = {1555 {\textendash} 1561}, abstract = {

Members of the ArsR/SmtB family of transcriptional repressors, such as CadC, regulate the intracellular levels of heavy metals like Cd(II), Hg(II), and Pb(II). These metal sensing proteins bind their target metals with high specificity and affinity, however, a lack of structural information about these proteins makes defining the coordination sphere of the target metal difficult. Lingering questions as to the identity of Cd(II) coordination in CadC are addressed via protein design techniques. Two designed peptides with tetrathiolate metal binding sites were prepared and characterized, revealing fast exchange between CdS3O and CdS4 coordination spheres. Correlation of (111m)Cd PAC spectroscopy and (113)Cd NMR spectroscopy suggests that Cd(II) coordinated to CadC is in fast exchange between CdS3O and CdS4 forms, which may provide a mechanism for rapid sensing of heavy metal contaminants by this regulatory protein.

}, doi = {10.1039/c5mt00228a}, author = {Tebo, Alison G and Hemmingsen, Lars and Pecoraro, Vincent L} } @article {65783, title = {Protein design: toward functional metalloenzymes.}, journal = {Chemical reviews}, volume = {114}, year = {2014}, month = {03/2014}, pages = {3495 {\textendash} 3578}, doi = {10.1021/cr400458x}, author = {Yu, Fangting and Cangelosi, Virginia M and Zastrow, Melissa L and Tegoni, Matteo and Plegaria, Jefferson S and Tebo, Alison G and Mocny, Catherine S and Ruckthong, Leela and Qayyum, Hira and Pecoraro, Vincent L} }