scholarly journals Correlation between computed gas-phase and experimentally determined solution-phase infrared spectra: Models of the iron–iron hydrogenase enzyme active site

2006 ◽  
Vol 27 (12) ◽  
pp. 1454-1462 ◽  
Author(s):  
Jesse W. Tye ◽  
Marcetta Y. Darensbourg ◽  
Michael B. Hall
Keyword(s):  
Gas Phase ◽  
Infrared Spectra ◽  
Active Site ◽  
Solution Phase ◽  
Enzyme Active Site ◽  
Iron Hydrogenase ◽  
Iron Iron ◽  
Hydrogenase Enzyme

Refining the Active Site Structure of Iron−Iron Hydrogenase Using Computational Infrared Spectroscopy

2008 ◽  
Vol 47 (7) ◽  
pp. 2380-2388 ◽  
Author(s):  
Jesse W. Tye ◽  
Marcetta Y. Darensbourg ◽  
Michael B. Hall
Keyword(s):  
Infrared Spectroscopy ◽  
Active Site ◽  
Site Structure ◽  
Iron Hydrogenase ◽  
Iron Iron ◽  
Active Site Structure

Electrocatalysis of hydrogen production by active site analogues of the iron hydrogenase enzyme: structure/function relationships

2003 ◽  
pp. 4158-4163 ◽  
Author(s):  
Daesung Chong ◽  
Irene P. Georgakaki ◽  
Rosario Mejia-Rodriguez ◽  
Jean Sanabria-Chinchilla ◽  
Manuel P. Soriaga ◽  
...  
Keyword(s):  
Hydrogen Production ◽  
Structure Function ◽  
Active Site ◽  
Enzyme Structure ◽  
Iron Hydrogenase ◽  
Hydrogenase Enzyme

Resin-bound models of the [FeFe]-hydrogenase enzyme active site and studies of their reactivity

2009 ◽  
pp. 4344 ◽  
Author(s):  
Kayla N. Green ◽  
Jennifer L. Hess ◽  
Christine M. Thomas ◽  
Marcetta Y. Darensbourg
Keyword(s):  
Active Site ◽  
Enzyme Active Site ◽  
Hydrogenase Enzyme

scholarly journals A mononuclear iron carbonyl complex [Fe(μ-bdt)(CO)2(PTA)2] with bulky phosphine ligands: a model for the [FeFe] hydrogenase enzyme active site with an inverted redox potential

2017 ◽  
Vol 46 (30) ◽  
pp. 10050-10056 ◽  
Author(s):  
M. Natarajan ◽  
H. Faujdar ◽  
S. M. Mobin ◽  
M. Stein ◽  
S. Kaur-Ghumaan
Keyword(s):  
Redox Potential ◽  
Hydrogen Evolution ◽  
Active Site ◽  
Acidic Solution ◽  
Iron Complex ◽  
Phosphine Ligands ◽  
Carbonyl Complex ◽  
Enzyme Active Site ◽  
Mononuclear Iron ◽  
Hydrogenase Enzyme

This mononuclear iron complex displays an inverted redox potential and catalyzes hydrogen evolution in acidic solution.

Sulfonated Diiron Complexes as Water-Soluble Models of the [Fe–Fe]-Hydrogenase Enzyme Active Site

2011 ◽  
Vol 50 (11) ◽  
pp. 5015-5026 ◽  
Author(s):  
Michael L. Singleton ◽  
Danielle J. Crouthers ◽  
Robert P. Duttweiler ◽  
Joseph H. Reibenspies ◽  
Marcetta Y. Darensbourg
Keyword(s):  
Active Site ◽  
Water Soluble ◽  
Enzyme Active Site ◽  
Hydrogenase Enzyme

Regioselective Gas-Phase n-Butane Transfer Dehydrogenation via Silica-Supported Pincer-Iridium Complexes

2020 ◽  
Author(s):  
Boris Sheludko ◽  
Cristina Castro ◽  
Chaitanya Khalap ◽  
Thomas Emge ◽  
Alan Goldman ◽  
...  
Keyword(s):  
Gas Phase ◽  
Active Site ◽  
Lower Cost ◽  
Open Systems ◽  
Iridium Complexes ◽  
Terminal Olefin ◽  
Molecular Precursors ◽  
Sterically Demanding ◽  
Olefin Production ◽  
Steam Cracking

<b>Abstract:</b> The production of olefins via on-purpose dehydrogenation of alkanes allows for a more efficient, selective and lower cost alternative to processes such as steam cracking. Silica-supported pincer-iridium complexes of the form [(≡SiO-<sup>R4</sup>POCOP)Ir(CO)] (<sup>R4</sup>POCOP = κ<sup>3</sup>-C<sub>6</sub>H<sub>3</sub>-2,6-(OPR<sub>2</sub>)<sub>2</sub>) are effective for acceptorless alkane dehydrogenation, and have been shown stable up to 300 °C. However, while solution-phase analogues of such species have demonstrated high regioselectivity for terminal olefin production under transfer dehydrogenation conditions at or below 240 °C, in open systems at 300 °C, regioselectivity under acceptorless dehydrogenation conditions is consistently low. In this work, complexes <a>[(≡SiO-<i><sup>t</sup></i><sup>Bu4</sup>POCOP)Ir(CO)] </a>(<b>1</b>) and [(≡SiO-<i><sup>i</sup></i><sup>Pr4</sup>PCP)Ir(CO)] (<b>2</b>) were synthesized via immobilization of molecular precursors. These complexes were used for gas-phase butane transfer dehydrogenation using increasingly sterically demanding olefins, resulting in observed selectivities of up to 77%. The results indicate that the active site is conserved upon immobilization.

scholarly journals Conformation-Specific Inhibitory Anti-MMP-7 Monoclonal Antibody Sensitizes Pancreatic Ductal Adenocarcinoma Cells to Chemotherapeutic Cell Kill

Cancers ◽  
2021 ◽  
Vol 13 (7) ◽  
pp. 1679
Author(s):  
Vishnu Mohan ◽  
Jean P. Gaffney ◽  
Inna Solomonov ◽  
Maxim Levin ◽  
Mordehay Klepfish ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Active Site ◽  
Drug Targets ◽  
Fas Ligand ◽  
Specific Activity ◽  
Matrix Metalloproteases ◽  
Ductal Adenocarcinoma ◽  
Enzyme Active Site ◽  
Induced Apoptosis

Matrix metalloproteases (MMPs) undergo post-translational modifications including pro-domain shedding. The activated forms of these enzymes are effective drug targets, but generating potent biological inhibitors against them remains challenging. We report the generation of anti-MMP-7 inhibitory monoclonal antibody (GSM-192), using an alternating immunization strategy with an active site mimicry antigen and the activated enzyme. Our protocol yielded highly selective anti-MMP-7 monoclonal antibody, which specifically inhibits MMP-7′s enzyme activity with high affinity (IC50 = 132 ± 10 nM). The atomic model of the MMP-7-GSM-192 Fab complex exhibited antibody binding to unique epitopes at the rim of the enzyme active site, sterically preventing entry of substrates into the catalytic cleft. In human PDAC biopsies, tissue staining with GSM-192 showed characteristic spatial distribution of activated MMP-7. Treatment with GSM-192 in vitro induced apoptosis via stabilization of cell surface Fas ligand and retarded cell migration. Co-treatment with GSM-192 and chemotherapeutics, gemcitabine and oxaliplatin elicited a synergistic effect. Our data illustrate the advantage of precisely targeting catalytic MMP-7 mediated disease specific activity.

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