Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Yelu Shi"'
Publikováno v:
Angewandte Chemie (International ed. in English). 61(45)
HNO has broad chemical and biomedical properties. Metal complexes and derivatives are widely used to make excellent HNO sensors. However, their favorable mechanistic origins are largely unknown. Cu cyclam is a useful platform to make excellent HNO se
Publikováno v:
Chemistry – A European Journal. 27:5019-5027
The interconversion of NO and HNO, via copper zinc superoxide dismutase (CuZnSOD), is important in biomedicine and for HNO detection. Many mechanistic questions, including the decades-long debate on reversibility, were resolved in this work. Calculat
Autor:
Yelu Shi, Erik R. Farquhar, Saumen Chakraborty, Pallavi Prasad, Skyler Crane, Dhanashree Selvan, Yong Zhang
Publikováno v:
ACS Catal
We report the construction of an artificial hydrogenase (ArH) by reengineering a Cu storage protein (Cspl) into a Ni-binding protein (NBP) employing rational metalloprotein design. The hypothesis driven design approach involved deleting existing Cu s
Autor:
Yelu Shi, Yong Zhang
Publikováno v:
Angewandte Chemie International Edition. 57:16654-16658
Many HNO scavenging pathways exist to regulate its in vivo and in vitro biological and pharmacological activities, including the involvement of numerous ferric heme proteins. Such reactions also build an important basis for HNO probe development. How
The oxygen reactivity of an artificial hydrogenase designed in a reengineered copper storage protein
Publikováno v:
Dalton Trans
The O(2) reactivity of an artificial biomolecular hydrogenase, the nickel binding protein (NBP) is investigated. Kinetic analyses revealed a complete 4e(−) reduction of O(2) to H(2)O under catalytic conditions with associated k(0) for ET in the ord
Autor:
Bing Wang, Leonard M. Thomas, Yelu Shi, Mark T. Gladwin, George B. Richter-Addo, Samantha M. Powell, Yong Zhang, Sruti Shiva, Jesús Tejero
Publikováno v:
Biochemistry. 57:4788-4802
The globular dioxygen binding heme protein myoglobin (Mb) is present in several species. Its interactions with the simple nitrogen oxides, namely, nitric oxide (NO) and nitrite, have been known for decades, but the physiological relevance has only re
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 (
Publikováno v:
Angewandte Chemie. 129:6722-6726
Heme-copper oxidase (HCO) is a class of respiratory enzymes that use a heme-copper center to catalyze O2 reduction to H2O. While heme reduction potential (E°′) of different HCO types has been found to vary >500 mV, its impact on HCO activity remai
HNO-Binding in Heme Proteins: Effects of Iron Oxidation State, Axial Ligand, and Protein Environment
Publikováno v:
Angewandte Chemie International Edition. 55:15058-15061
HNO plays significant roles in many biological processes. Numerous heme proteins bind HNO, an important step for its biological functions. A systematic computational study was performed to provide the first detailed trends and origins of the effects
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