Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Evan N. Mirts"'
Publikováno v:
Angewandte Chemie. 135
Engineering enzymes with novel reactivity and applying them in metabolic pathways to produce valuable products are quite challenging due to the intrinsic complexity of metabolic networks and the need for high in vivo catalytic efficiency. Triacetic a
Publikováno v:
Accounts of Chemical Research. 52:935-944
Metalloproteins set the gold standard for performing important functions, including catalyzing demanding reactions under mild conditions. Designing artificial metalloenzymes (ArMs) to catalyze abiological reactions has been a major endeavor for many
Publikováno v:
Science. 361:1098-1101
Metals brought together do more Enzymatic reduction of oxyanions such as sulfite (SO 3 2− ) requires the delivery of multiple electrons and protons, a feat accomplished by cofactors tailored for catalysis and electron transport. Replicating this st
Publikováno v:
Chem Soc Rev
Heme-copper oxidases (HCO), nitric oxide reductases (NOR), and sulfite reductases (SiR) catalyze the multi-electron and multi-proton reductions of O(2), NO, and SO(3)(2−), respectively. Each of these reactions is important to drive cellular energy
Publikováno v:
J Am Chem Soc
The primary and secondary coordination spheres of metal binding sites in metalloproteins have been investigated extensively, leading to the creation of high-performing functional metalloproteins; however, the impact of the overall structure of the pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f2b2ebbd1e163900981396ebbbc0d2b5
https://europepmc.org/articles/PMC8168375/
https://europepmc.org/articles/PMC8168375/
Autor:
Pierre Moënne-Loccoz, Shuyan Wang, Braddock A. Sandoval, Yelu Shi, Yi Lu, Yong Zhang, Julian Reed, Evan N. Mirts, Ambika Bhagi-Damodaran, Madeline R. Sponholtz, Kevin A. Harnden, Parisa Hosseinzadeh, Sudharsan Dwaraknath, Qianhong Zhu
Publikováno v:
Proceedings of the National Academy of Sciences. 115:6195-6200
Despite high structural homology between NO reductases (NORs) and heme-copper oxidases (HCOs), factors governing their reaction specificity remain to be understood. Using a myoglobin-based model of NOR (Fe B Mb) and tuning its heme redox potentials (
Autor:
Pierre Moënne-Loccoz, Evan N. Mirts, Matthew A. Michael, Yong Zhang, Yi Lu, Braddock A. Sandoval, Ambika Bhagi-Damodaran, Saumen Chakraborty, Qianhong Zhu, Julian Reed
Publikováno v:
Nature Chemistry. 9:257-263
Haem-copper oxidase (HCO) catalyses the natural reduction of oxygen to water using a haem-copper centre. Despite decades of research on HCOs, the role of non-haem metal and the reason for nature's choice of copper over other metals such as iron remai
Publikováno v:
Dioxygen-dependent Heme Enzymes ISBN: 9781782629917
O2-dependent heme enzymes such as oxidases and oxygenases play important roles in numerous biological processes and much progress has been made in understanding structural features responsible for their diverse and efficient functions. An ultimate te
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8e996cc4412328d23572a1d89b1a681d
https://doi.org/10.1039/9781788012911-00037
https://doi.org/10.1039/9781788012911-00037
Autor:
Yi Lu, Thomas D. Pfister, Christopher G. Mayne, Evan N. Mirts, Emad Tajkhorshid, Howard Robinson, Parisa Hosseinzadeh, Yi Gui Gao
Publikováno v:
Biochemistry. 55:1494-1502
Noncovalent second-shell interactions are important in controlling metal-binding affinity and activity in metalloenzymes, but fine-tuning these interactions in designed metalloenzymes has not been fully explored. As a result, most designed metalloenz
Autor:
Matthew O. Ross, Igor D. Petrik, Pierre Moënne-Loccoz, Yelu Shi, Yi Lu, Qianhong Zhu, Ambika Bhagi-Damodaran, Julian Reed, Yong Zhang, Saumen Chakraborty, Evan N. Mirts
Publikováno v:
Journal of the American Chemical Society. 139(35)
The presence of nonheme metal, such as copper and iron, in the heme-copper oxidase (HCO) superfamily is critical to the enzymatic activity of reducing O2 to H2O, but the exact mechanism the nonheme metal ion uses to confer and fine-tune the activity