| Bridging the gap between chemistry, physiology, and evolution: Quantifying the functionality of sperm whale myoglobin mutants. | |
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MedLine Citation:
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PMID: 21903173 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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This work merges a large set of previously reported thermochemical data for myoglobin (Mb) mutants with a physiological model of O(2)-transport and -storage. The model allows a quantification of the functional proficiency of myoglobin (Mb) mutants under various physiological conditions, i.e. O(2)-consumption rate resembling workload, O(2) partial pressure resembling hypoxic stress, muscle cell size, and Mb concentration, resembling different organism-specific and compensatory variables. We find that O(2)-storage and -transport are distinct functions that rank mutants and wild type differently depending on O(2) partial pressure. Specifically, the wild type is near-optimal for storage at all conditions, but for transport only at severely hypoxic conditions. At normoxic conditions, low-affinity mutants are in fact better O(2)-transporters because they still have empty sites for O(2), giving rise to a larger [MbO(2)] gradient (more varying saturation curve). The distributions of functionality reveal that many mutants are near-neutral with respect to function, whereas only a few are strongly affected, and the variation in functionality increases dramatically at lower O(2) pressure. These results together show that conserved residues in wild type (WT) Mb were fixated under a selection pressure of low P(O2). |
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Authors:
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Pouria Dasmeh; Kasper P Kepp |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2011-8-8 |
Journal Detail:
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Title: Comparative biochemistry and physiology. Part A, Molecular & integrative physiology Volume: - ISSN: 1531-4332 ISO Abbreviation: - Publication Date: 2011 Aug |
Date Detail:
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Created Date: 2011-9-9 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 9806096 Medline TA: Comp Biochem Physiol A Mol Integr Physiol Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Copyright Information:
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Copyright © 2011. Published by Elsevier Inc. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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