Bing Wang1, Leonard M Thomas1, George B Richter-Addo2. 1. Department of Chemistry and Biochemistry, and Price Family Foundation Institute of Structural Biology, University of Oklahoma, Norman 73019, United States. 2. Department of Chemistry and Biochemistry, and Price Family Foundation Institute of Structural Biology, University of Oklahoma, Norman 73019, United States. Electronic address: grichteraddo@ou.edu.
Abstract
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 1.7-1.9Å 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.
Bioorganometallic Fe-C bonds are biologically relevant species that may result from the metabolism of natural or synthetic n class="Chemical">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 1.7-1.9Å 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.
Authors: Bing Wang; Yelu Shi; Jesús Tejero; Samantha M Powell; Leonard M Thomas; Mark T Gladwin; Sruti Shiva; Yong Zhang; George B Richter-Addo Journal: Biochemistry Date: 2018-07-27 Impact factor: 3.162