The use of a cis-dioxomolybdenum(VI) dinuclear complex with quadradentate 1,4-benzenediylbis(benzyldithiocarbamate)(2−) as model compound for the active site of oxo transfer molybdoenzymes: Reactivity, kinetics, and catalysis

2012 ◽  
Vol 88 ◽  
pp. 210-215 ◽  
Author(s):  
Zeinab Moradi-Shoeili ◽  
Davar M. Boghaei
Keyword(s):  
Active Site ◽  
Model Compound ◽  
Dinuclear Complex ◽  
Oxo Transfer

Model compound of [FeFe]-hydrogenase active site employing [2Fe–2S] subunit as non-innocent [4Fe–4S] cluster and its proton reduction performance

2020 ◽  
Vol 45 (21) ◽  
pp. 11995-11999 ◽  
Author(s):  
Li Hai ◽  
Tianyong Zhang ◽  
Shuang Jiang ◽  
Xia Zhang ◽  
Guanghui Zhang ◽  
...  
Keyword(s):  
Active Site ◽  
Model Compound ◽  
Proton Reduction

Reduction of ormaplatin by a dithiol model compound for the active site of thioredoxin: stopped-flow kinetic analysis

2015 ◽  
Vol 40 (4) ◽  
pp. 347-353 ◽  
Author(s):  
Yanli Ren ◽  
Jingran Dong ◽  
Hongmei Shi ◽  
Shuying Huo ◽  
Tingting Dai ◽  
...  
Keyword(s):  
Kinetic Analysis ◽  
Active Site ◽  
Model Compound ◽  
Stopped Flow

Kinetic studies of pepsin active site model compound and porcine pepsin

2001 ◽  
Vol 14 (2) ◽  
pp. 103-108 ◽  
Author(s):  
Bogdan Swoboda ◽  
Maria Be?towska-Brzezinska ◽  
Grzegorz Schroeder ◽  
Bogumil Brzezinski ◽  
Georg Zundel
Keyword(s):  
Active Site ◽  
Model Compound ◽  
Kinetic Studies ◽  
Porcine Pepsin ◽  
Site Model ◽  
Active Site Model

Multiple-Timescale Photoreactivity of a Model Compound Related to the Active Site of [FeFe]-Hydrogenase

2008 ◽  
Vol 47 (17) ◽  
pp. 7453-7455 ◽  
Author(s):  
Anna R. Ridley ◽  
A. Ian Stewart ◽  
Katrin Adamczyk ◽  
Hirendra N. Ghosh ◽  
Boutheïna Kerkeni ◽  
...  
Keyword(s):  
Active Site ◽  
Model Compound ◽  
Multiple Timescale

scholarly journals Model compound met the key structural and spectroscopic features of [FeFe]-hydrogenase active site

2019 ◽  
Author(s):  
Li Hai ◽  
Tianyong Zhang ◽  
Shuang Jiang ◽  
Xiaoyuan Ma ◽  
Di Wang ◽  
...  
Keyword(s):  
Active Site ◽  
Model Compound ◽  
Catalytic Efficiency ◽  
Biomimetic Synthesis ◽  
Reversible Transition ◽  
Oxidation Potentials ◽  
Open Site ◽  
Structural Aspects

Biomimetic synthesis of the [FeFe]-hydrogenase active site draws considerable attention of scientists for its amazing catalytic efficiency on reversible transition between proton and hydrogen. Fe2(CO)3[μ-(SCH(CH2CH3)CH2S)](μ-DPPM)(κ1-DPPM) (compound 1) which replicated key structural aspects of the natural [FeFe]-hydrogenase was designed and synthesized. 1 showed that the wavenumbers in IR were close to those of the natural [FeFe]-hydrogenase active site. In addition, 1 achieved the low oxidation potentials at -0.48 V and -0.26 V, respectively. In the assistance of ethyl located in the S-S bridging structure, the asymmetrical substitution with sterically encumbering and electron-rich ligands in 1 may offer a thorough protection for forming and stabilizing the open site in the rotated structure.

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