5ilm: Difference between revisions
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/MYG_PHYCD MYG_PHYCD]] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles. | [[http://www.uniprot.org/uniprot/MYG_PHYCD MYG_PHYCD]] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles. | ||
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== Publication Abstract from PubMed == | |||
Bioorganometallic Fe-C bonds are biologically relevant species that may result from the metabolism of natural or synthetic hydrazines. The molecular structures of four new sperm whale mutant myoglobin derivatives with Fe-aryl moieties, namely H64A-tolyl-m, H64A-chlorophenyl-p, H64Q-tolyl-m, and H64Q-chlorophenyl-p, have been determined at 1.7-1.9A resolution. The structures reveal conformational preferences for the substituted aryls resulting from attachment of the aryl ligands to Fe at the site of net -NHNH2 release from the precursor hydrazines, and show distal pocket changes that readily accommodate these bulky ligands. | |||
Organometallic myoglobins: Formation of Fe-carbon bonds and distal pocket effects on aryl ligand conformations.,Wang B, Thomas LM, Richter-Addo GB J Inorg Biochem. 2016 Jun 24. pii: S0162-0134(16)30192-1. doi:, 10.1016/j.jinorgbio.2016.06.028. PMID:27687333<ref>PMID:27687333</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 09:58, 19 October 2016
H64A sperm whale myoglobin with a Fe-chlorophenyl moiety
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