Mineral Surfaces as Agents of Environmental Proteolysis: Mechanisms and Controls

Chacon, Stephany S.; Reardon, Patrick N.; Burgess, Christopher J.; Purvine, Samuel; Chu, Rosalie K.; Clauss, Therese R.; Walter, Eric; Myrold, David D.; Washton, Nancy; Kleber, Markus

doi:10.1021/acs.est.8b05583

Title: Mineral Surfaces as Agents of Environmental Proteolysis: Mechanisms and Controls

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Abstract

We investigated the extent to which contact with mineral surfaces affected the molecular integrity of a model protein, with an emphasis on identifying the mechanisms (hydrolysis, oxidation) and conditions leading to protein alteration. To this end, we studied the ability of four mineral surface archetypes (negatively charged, positively charged, neutral, redox-active) to abiotically fragment a well characterized protein (GB1) as a function of pH and contact time. GB1 was exposed to the soil minerals montmorillonite, goethite, kaolinite, and birnessite at pH 5 and pH 7 for 1, 8, 24, and 168 h and the supernatant was screened for peptide fragments using Tandem Mass Spectrometry. To distinguish between products of oxidative and hydrolytic cleavage, we combined results from the SEQUEST algorithm, which identifies protein fragments that were cleaved hydrolytically, with the output of a deconvolution algorithm (DECON-Routine) designed to identify oxidation fragments. All four minerals were able to induce protein cleavage. Manganese oxide was effective at both hydrolytic and oxidative cleavage. The fact that phyllosilicates?which are not redox active?induced oxidative cleavage indicates that surfaces acted as catalysts and not as reactants. Our results extend previous observations of proteolytic capabilities in soil minerals to the groups of phyllosilicates and Fe-oxides. We identifiedmore »« less

Authors:

^[1]; Reardon, Patrick N. ^[2]; Burgess, Christopher J. ^[3];

^[4]; Chu, Rosalie K. ^[4]; Clauss, Therese R. ^[4];

^[4]; Myrold, David D. ^[3]; Washton, Nancy ^[4]; Kleber, Markus ^[3]

Oregon State Univ., Corvallis, OR (United States); Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
Pacific Northwest National Lab. (PNNL), Richland, WA (United States); Oregon State Univ., Corvallis, OR (United States)
Oregon State Univ., Corvallis, OR (United States)
Pacific Northwest National Lab. (PNNL), Richland, WA (United States)

Publication Date:: Fri Feb 15 00:00:00 EST 2019

Research Org.:: Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States); Pacific Northwest National Lab. (PNNL), Richland, WA (United States)

Sponsoring Org.:: USDOE Office of Science (SC), Biological and Environmental Research (BER); USDOE Office of Science (SC), Workforce Development for Teachers and Scientists (WDTS)

OSTI Identifier:: 1503671

Alternate Identifier(s):: OSTI ID: 1523191

Report Number(s):: PNNL-SA-141783
Journal ID: ISSN 0013-936X; ark:/13030/qt0dp5386b

Grant/Contract Number:: AC02-05CH11231; AC05-76RL01830

Resource Type:: Accepted Manuscript

Journal Name:: Environmental Science and Technology

Additional Journal Information:: Journal Volume: 53; Journal Issue: 6; Journal ID: ISSN 0013-936X

Publisher:: American Chemical Society (ACS)

Country of Publication:: United States

Language:: English

Subject:: 54 ENVIRONMENTAL SCIENCES; protein, protein fragmentation, mineral surfaces, bioavailability, proteomics

Citation Formats


                    Chacon, Stephany S., Reardon, Patrick N., Burgess, Christopher J., Purvine, Samuel, Chu, Rosalie K., Clauss, Therese R., Walter, Eric, Myrold, David D., Washton, Nancy, and Kleber, Markus. Mineral Surfaces as Agents of Environmental Proteolysis: Mechanisms and Controls.  United States: N. p., 2019. 
Web.  doi:10.1021/acs.est.8b05583.

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                    Chacon, Stephany S., Reardon, Patrick N., Burgess, Christopher J., Purvine, Samuel, Chu, Rosalie K., Clauss, Therese R., Walter, Eric, Myrold, David D., Washton, Nancy, & Kleber, Markus. Mineral Surfaces as Agents of Environmental Proteolysis: Mechanisms and Controls.  United States.  https://doi.org/10.1021/acs.est.8b05583

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                    Chacon, Stephany S., Reardon, Patrick N., Burgess, Christopher J., Purvine, Samuel, Chu, Rosalie K., Clauss, Therese R., Walter, Eric, Myrold, David D., Washton, Nancy, and Kleber, Markus. Fri .  
"Mineral Surfaces as Agents of Environmental Proteolysis: Mechanisms and Controls".  United States.  https://doi.org/10.1021/acs.est.8b05583.  https://www.osti.gov/servlets/purl/1503671.

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@article{osti_1503671,

  title        = {Mineral Surfaces as Agents of Environmental Proteolysis: Mechanisms and Controls},

  author       = {Chacon, Stephany S. and Reardon, Patrick N. and Burgess, Christopher J. and Purvine, Samuel and Chu, Rosalie K. and Clauss, Therese R. and Walter, Eric and Myrold, David D. and Washton, Nancy and Kleber, Markus},

  abstractNote = {We investigated the extent to which contact with mineral surfaces affected the molecular integrity of a model protein, with an emphasis on identifying the mechanisms (hydrolysis, oxidation) and conditions leading to protein alteration. To this end, we studied the ability of four mineral surface archetypes (negatively charged, positively charged, neutral, redox-active) to abiotically fragment a well characterized protein (GB1) as a function of pH and contact time. GB1 was exposed to the soil minerals montmorillonite, goethite, kaolinite, and birnessite at pH 5 and pH 7 for 1, 8, 24, and 168 h and the supernatant was screened for peptide fragments using Tandem Mass Spectrometry. To distinguish between products of oxidative and hydrolytic cleavage, we combined results from the SEQUEST algorithm, which identifies protein fragments that were cleaved hydrolytically, with the output of a deconvolution algorithm (DECON-Routine) designed to identify oxidation fragments. All four minerals were able to induce protein cleavage. Manganese oxide was effective at both hydrolytic and oxidative cleavage. The fact that phyllosilicates?which are not redox active?induced oxidative cleavage indicates that surfaces acted as catalysts and not as reactants. Our results extend previous observations of proteolytic capabilities in soil minerals to the groups of phyllosilicates and Fe-oxides. We identified structural regions of the protein with particularly high susceptibility to cleavage (loops and ß strands) as well as regions that were entirely unaffected (a helix).},

  doi          = {10.1021/acs.est.8b05583},

  journal      = {Environmental Science and Technology},

  number       = 6,

  volume       = 53,

  place        = {United States},

  year         = {Fri Feb 15 00:00:00 EST 2019},

  month        = {Fri Feb 15 00:00:00 EST 2019}

}

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