Angewandte Chemie International Edition, 2012 Apr 27;51(18):4312-6. doi: 10.1002/anie.201108756. Epub 2012 Mar 12.
Significant increase of oxidase activity through the genetic incorporation of a tyrosine-histidine cross-link in a myoglobin model of heme-copper oxidase.
Liu X, Yu Y, Hu C, Zhang W, Lu Y, Wang J.
SourceLaboratory of Noncoding RNA, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang District, Beijing, 100101, China.
Abstract
In aerobic respiration, heme–copper oxidase1 (HCO) performs efficient four-electron reduction of oxygen to water without releasing toxic, reactive oxygen species (ROS) such as superoxide and peroxide.2 Because of its importance in biogenetics, fascinating chemistry, and potential applications in fuel cells, HCO has been intensively investigated by structural biologists,3 enzymologists,1,?4 and synthetic chemists.5 While tremendous progress has been made from the above studies, several important questions about the structural features and mechanism of HCO still remain. Of particular interest is the unique post-translationally modified covalent cross-link between carbon atom C6 of a tyrosine residue and nitrogen atom Nε2 of a nearby histidine residue (Tyr–His cross-link, Figure?1?A), which was first revealed by a high-resolution X-ray structure3a and then confirmed by biochemical and biophysical studies.6 Importantly, the Tyr–His cross-link is conserved in bacterial and mammal HCOs,5b thus implicating a strong evolutionary connection and the functional significance of the cross-link.
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全文链接：http://dx.doi.org/10.1002/anie.201108756
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