Redox Characterization of Electrode-Immobilized Bacterial Microcompartment Shell Proteins Engineered To Bind Metal Centers

2019 ◽  
Vol 3 (1) ◽  
pp. 685-692 ◽  
Author(s):  
Jefferson S. Plegaria ◽  
Matthew D. Yates ◽  
Sarah M. Glaven ◽  
Cheryl A. Kerfeld
Keyword(s):  
Metal Centers ◽  
Bacterial Microcompartment ◽  
Shell Proteins

Structural characterization of hexameric shell proteins from two types of choline-utilization bacterial microcompartments

2021 ◽  
Vol 77 (9) ◽  
Author(s):  
Jessica M. Ochoa ◽  
Oscar Mijares ◽  
Andrea A. Acosta ◽  
Xavier Escoto ◽  
Nancy Leon-Rivera ◽  
...  
Keyword(s):  
Structural Characterization ◽  
Building Blocks ◽  
Type I ◽  
Type Ii ◽  
Protein Subunits ◽  
Bacterial Microcompartments ◽  
Bacterial Microcompartment ◽  
Glycyl Radical ◽  
Shell Proteins

Bacterial microcompartments are large supramolecular structures comprising an outer proteinaceous shell that encapsulates various enzymes in order to optimize metabolic processes. The outer shells of bacterial microcompartments are made of several thousand protein subunits, generally forming hexameric building blocks based on the canonical bacterial microcompartment (BMC) domain. Among the diverse metabolic types of bacterial microcompartments, the structures of those that use glycyl radical enzymes to metabolize choline have not been adequately characterized. Here, six structures of hexameric shell proteins from type I and type II choline-utilization microcompartments are reported. Sequence and structure analysis reveals electrostatic surface properties that are shared between the four types of shell proteins described here.

Engineering Bacterial Microcompartment Shells: Chimeric Shell Proteins and Chimeric Carboxysome Shells

2014 ◽  
Vol 4 (4) ◽  
pp. 444-453 ◽  
Author(s):  
Fei Cai ◽  
Markus Sutter ◽  
Susan L. Bernstein ◽  
James N. Kinney ◽  
Cheryl A. Kerfeld
Keyword(s):  
Bacterial Microcompartment ◽  
Shell Proteins

scholarly journals Functionalization of Bacterial Microcompartment Shell Proteins With Covalently Attached Heme

2020 ◽  
Vol 7 ◽  
Author(s):  
Jingcheng Huang ◽  
Bryan H. Ferlez ◽  
Eric J. Young ◽  
Cheryl A. Kerfeld ◽  
David M. Kramer ◽  
...  
Keyword(s):  
Bacterial Microcompartment ◽  
Shell Proteins

Metallacycles with Stereogenic Metal Centers: Synthesis and Characterization of Diastereomeric Cycloruthenated Chiral Amines

1995 ◽  
Vol 14 (10) ◽  
pp. 4559-4569 ◽  
Author(s):  
Saeed Attar ◽  
John H. Nelson ◽  
Jean Fischer ◽  
Andre de Cian ◽  
Jean-Pascal Sutter ◽  
...  
Keyword(s):  
Synthesis And Characterization ◽  
Chiral Amines ◽  
Metal Centers

scholarly journals Coordination polymers of benzenediseleninate, the seleno analog of terephthalate

2014 ◽  
Vol 70 (a1) ◽  
pp. C1235-C1235
Author(s):  
Robert Burrow ◽  
Giancarlo Belmonte
Keyword(s):  
Coordination Polymers ◽  
Water Molecules ◽  
Gravimetric Analysis ◽  
The Novel ◽  
X Ray Diffraction ◽  
Reaction Conditions ◽  
Subsequent Formation ◽  
Metal Centers ◽  
Infrared Spectral

The proligand para-benzenediseleninic acid, (HO2SeC6H4SeO2H) (Figure), is the seleno analog to the commonly used MOF spacer proligand, terephthalic acid. Novel coordination polymers based on this proligand, and Mn(II), Fe(II), Co(II), Ni(II), Cu(II) or Zn(II) metal centers containing auxiliary water molecules, [M(O2SeC6H4SeO2)2(H2O)n], were synthesized. Depending on the reaction conditions, different pure or mixed phases can be produced. Crystal to crystal transformations of the novel coordination polymers were studied with powder X ray diffraction, infrared spectral analysis and thermal gravimetric analysis. These coordination polymers can be dehydrated with subsequent formation of new anhydrous coordination polymer phases. Some of these phases can be rehydrated to lead back to the crystalline starting materials or to new crystalline hydrated phases. We are working on the complete structural characterization of the phases.

scholarly journals Characterization of the Particulate Methane Monooxygenase Metal Centers in Multiple Redox States by X-ray Absorption Spectroscopy

2006 ◽  
Vol 45 (20) ◽  
pp. 8372-8381 ◽  
Author(s):  
Raquel L. Lieberman ◽  
Kalyan C. Kondapalli ◽  
Deepak B. Shrestha ◽  
Amanda S. Hakemian ◽  
Stephen M. Smith ◽  
...  
Keyword(s):  
Absorption Spectroscopy ◽  
Methane Monooxygenase ◽  
Particulate Methane Monooxygenase ◽  
Metal Centers ◽  
X Ray ◽  
Redox States ◽  
X Ray Absorption

scholarly journals Synthesis and Characterization of New Cyclam-Based Zr(IV) Alkoxido Derivatives

Reactions ◽  
2021 ◽  
Vol 2 (3) ◽  
pp. 323-332
Author(s):  
Luis G. Alves ◽  
Ana M. Martins
Keyword(s):  
Carbon Dioxide ◽  
Solid State ◽  
Molecular Structures ◽  
Synthesis And Characterization ◽  
Metal Centers ◽  
Trigonal Prismatic

In this study, new mono- and di-alkoxido zirconium(IV) complexes supported by tetradentate dianionic cyclam ligands were synthesized and characterized. These compounds were obtained by reaction of the parent Zr(IV) dichlorido species with one or two equivalents of the corresponding lithium alkoxido, whereas (3,5-Me2Bn2Cyclam)Zr(OPh)2 was prepared by protonolysis of the orthometallated species (3,5-Me-C6H4CH2)2Cyclam)Zr with phenol. The solid-state molecular structures of (Bn2Cyclam)ZrCl(OtBu) and (4-tBuBn2Cyclam)Zr(OiPr)2 show a trigonal prismatic geometry around the metal centers. (Bn2Cyclam)Zr(SPh)(OtBu) and (Bn2Cyclam)ZrMe(OiPr) were prepared by reaction of (Bn2Cyclam)ZrCl(OR) (R = iPr, tBu) with one equivalent of LiSPh or MeMgCl, respectively. The reactions of (Bn2Cyclam)Zr(OiPr)2 and (4-tBuBn2Cyclam)Zr(OiPr)2 with carbon dioxide suggested the formation of species that correspond to the addition of four CO2 molecules.

scholarly journals Engineered shell proteins confer improved encapsulated pathway behavior in a bacterial microcompartment

2017 ◽  
Author(s):  
Marilyn F. Slininger Lee ◽  
Christopher M. Jakobson ◽  
Danielle Tullman-Ercek
Keyword(s):  
Growth Enhancement ◽  
Shell Protein ◽  
Bacterial Microcompartment ◽  
Hydropathy Index ◽  
Shell Proteins ◽  
Structure Result ◽  
Pore Lining ◽  
Protein Shell ◽  
Control Diffusion ◽  
Do So

AbstractBacterial microcompartments are a class of proteinaceous organelles comprising a characteristic protein shell enclosing a set of enzymes. Compartmentalization can prevent escape of volatile or toxic intermediates, prevent off-pathway reactions, and create private cofactor pools. Encapsulation in synthetic microcompartment organelles will enhance the function of heterologous pathways, but to do so, it is critical to understand how to control diffusion in and out of the microcompartment organelle. To this end, we explored how small differences in the shell protein structure result in changes in the diffusion of metabolites through the shell. We found that the ethanolamine utilization (Eut) protein EutM properly incorporates into the 1,2-propanediol utilization (Pdu) microcompartment, altering native metabolite accumulation and the resulting growth on 1,2-propanediol as the sole carbon source. Further, we identified a single pore-lining residue mutation that confers the same phenotype as substitution of the full EutM protein, indicating that small molecule diffusion through the shell is the cause of growth enhancement. Finally, we show that the hydropathy index and charge of pore amino acids are important indicators to predict how pore mutations will affect growth on 1,2- propanediol, likely by controlling diffusion of one or more metabolites. This study highlights the success of two strategies to engineer microcompartment control over metabolite transport: altering the existing shell protein pore via mutation of the pore-lining residues, and generating chimeras using shell proteins with the desired pores.TOC Abstract Graphic

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