| Modulating heme redox potential through protein-induced porphyrin distortion. | |
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MedLine Citation:
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PMID: 20735135 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Hemoproteins are ubiquitous in biology and are commonly involved in critical processes such as electron transfer, oxidative phosphorylation, and signal transduction. Both the protein environment and the heme cofactor contribute to generate the range of chemical properties needed for these diverse functions. Using the heme nitric oxide/oxygen binding (H-NOX) protein from the thermophilic bacterium Thermoanaerobacter tengcongensis, we have shown that heme electronic properties can be modulated by porphyrin distortion within the same protein scaffold without changing the heme ligation state or heme environment. The degree of heme distortion was found to be directly correlated to the electron density at the heme iron, as evidenced by dramatic changes in the heme redox potential and pK(a) of the distal ligand ((-)OH vs H(2)O). Protein-induced porphyrin distortion represents a new strategy to rationally tune the electronic properties of protein-bound porphyrins and could be used to engineer proteins with desired reactivity or functionality. |
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Authors:
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Charles Olea; John Kuriyan; Michael A Marletta |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural |
Journal Detail:
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Title: Journal of the American Chemical Society Volume: 132 ISSN: 1520-5126 ISO Abbreviation: J. Am. Chem. Soc. Publication Date: 2010 Sep |
Date Detail:
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Created Date: 2010-09-15 Completed Date: 2011-01-04 Revised Date: 2012-04-26 |
Medline Journal Info:
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Nlm Unique ID: 7503056 Medline TA: J Am Chem Soc Country: United States |
Other Details:
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Languages: eng Pagination: 12794-5 Citation Subset: IM |
Affiliation:
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Department of Molecular and Cell Biology, California Institute for Quantitative Biosciences, and Division of Physical Biosciences, University of California, Berkeley, Berkeley, California 94720-3220, USA. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Bacterial Proteins
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chemistry*,
genetics,
metabolism* Heme / chemistry*, metabolism* Hydrophobic and Hydrophilic Interactions Ligands Models, Molecular Molecular Conformation* Mutagenesis, Site-Directed Oxidation-Reduction Thermoanaerobacter |
| Grant Support | |
ID/Acronym/Agency:
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GM070671/GM/NIGMS NIH HHS; R01 GM070671-04/GM/NIGMS NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Bacterial Proteins; 0/Ligands; 14875-96-8/Heme |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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