Effect of the protonation degree of a self-assembled monolayer on the immobilization dynamics of a [NiFe] hydrogenase
Understanding the interaction and immobilization of [NiFe] hydrogenases on functionalized surfaces is important in the field of biotechnology and, in particular, for the development of biofuel cells. In this study, we investigated the adsorption behavior of the standard [NiFe] hydrogenase of Desulfo...
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paper:paper_07437463_v29_n2_p673_Utesch2023-06-08T15:45:01Z Effect of the protonation degree of a self-assembled monolayer on the immobilization dynamics of a [NiFe] hydrogenase Castro, Maria Ana [NiFe]-hydrogenase Adsorption behavior Adsorption mechanism Alkanethiols Amino-terminated Atomic levels Chemically modified electrode Desulfovibrio Desulfovibrio vulgaris Functionalized surfaces Gigas Highly-ionized Hydrogenases Initial adsorption Low degree Molecular dynamics simulations Protonation degree Sams Strong correlation Surface-enhanced infrared absorptions Adsorption Fluorine Ionization Light absorption Molecular dynamics Protonation Self assembled monolayers Organic polymers alkane bacterial protein gold hydrogenase immobilized protein nickel iron hydrogenase nickel-iron hydrogenase proton thiol derivative adsorption article chemistry Desulfovibrio gigas Desulfovibrio vulgaris electrode enzymology kinetics molecular dynamics pH thermodynamics Adsorption Alkanes Bacterial Proteins Desulfovibrio gigas Desulfovibrio vulgaris Electrodes Gold Hydrogen-Ion Concentration Hydrogenase Immobilized Proteins Kinetics Molecular Dynamics Simulation Protons Sulfhydryl Compounds Thermodynamics Understanding the interaction and immobilization of [NiFe] hydrogenases on functionalized surfaces is important in the field of biotechnology and, in particular, for the development of biofuel cells. In this study, we investigated the adsorption behavior of the standard [NiFe] hydrogenase of Desulfovibrio gigas on amino-terminated alkanethiol self-assembled monolayers (SAMs) with different levels of protonation. Classical all-atom molecular dynamics (MD) simulations revealed a strong correlation between the adsorption behavior and the level of ionization of the chemically modified electrode surface. While the hydrogenase undergoes a weak but stable initial adsorption process on SAMs with a low degree of protonation, a stronger immobilization is observable on highly ionized SAMs, affecting protein reorientation and conformation. These results were validated by complementary surface-enhanced infrared absorption (SEIRA) measurements on the comparable [NiFe] standard hydrogenases from Desulfovibrio vulgaris Miyazaki F and allowed in this way for a detailed insight into the adsorption mechanism at the atomic level. © 2012 American Chemical Society. Fil:Castro, M.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2013 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_07437463_v29_n2_p673_Utesch http://hdl.handle.net/20.500.12110/paper_07437463_v29_n2_p673_Utesch |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
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R-134 |
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
[NiFe]-hydrogenase Adsorption behavior Adsorption mechanism Alkanethiols Amino-terminated Atomic levels Chemically modified electrode Desulfovibrio Desulfovibrio vulgaris Functionalized surfaces Gigas Highly-ionized Hydrogenases Initial adsorption Low degree Molecular dynamics simulations Protonation degree Sams Strong correlation Surface-enhanced infrared absorptions Adsorption Fluorine Ionization Light absorption Molecular dynamics Protonation Self assembled monolayers Organic polymers alkane bacterial protein gold hydrogenase immobilized protein nickel iron hydrogenase nickel-iron hydrogenase proton thiol derivative adsorption article chemistry Desulfovibrio gigas Desulfovibrio vulgaris electrode enzymology kinetics molecular dynamics pH thermodynamics Adsorption Alkanes Bacterial Proteins Desulfovibrio gigas Desulfovibrio vulgaris Electrodes Gold Hydrogen-Ion Concentration Hydrogenase Immobilized Proteins Kinetics Molecular Dynamics Simulation Protons Sulfhydryl Compounds Thermodynamics |
| spellingShingle |
[NiFe]-hydrogenase Adsorption behavior Adsorption mechanism Alkanethiols Amino-terminated Atomic levels Chemically modified electrode Desulfovibrio Desulfovibrio vulgaris Functionalized surfaces Gigas Highly-ionized Hydrogenases Initial adsorption Low degree Molecular dynamics simulations Protonation degree Sams Strong correlation Surface-enhanced infrared absorptions Adsorption Fluorine Ionization Light absorption Molecular dynamics Protonation Self assembled monolayers Organic polymers alkane bacterial protein gold hydrogenase immobilized protein nickel iron hydrogenase nickel-iron hydrogenase proton thiol derivative adsorption article chemistry Desulfovibrio gigas Desulfovibrio vulgaris electrode enzymology kinetics molecular dynamics pH thermodynamics Adsorption Alkanes Bacterial Proteins Desulfovibrio gigas Desulfovibrio vulgaris Electrodes Gold Hydrogen-Ion Concentration Hydrogenase Immobilized Proteins Kinetics Molecular Dynamics Simulation Protons Sulfhydryl Compounds Thermodynamics Castro, Maria Ana Effect of the protonation degree of a self-assembled monolayer on the immobilization dynamics of a [NiFe] hydrogenase |
| topic_facet |
[NiFe]-hydrogenase Adsorption behavior Adsorption mechanism Alkanethiols Amino-terminated Atomic levels Chemically modified electrode Desulfovibrio Desulfovibrio vulgaris Functionalized surfaces Gigas Highly-ionized Hydrogenases Initial adsorption Low degree Molecular dynamics simulations Protonation degree Sams Strong correlation Surface-enhanced infrared absorptions Adsorption Fluorine Ionization Light absorption Molecular dynamics Protonation Self assembled monolayers Organic polymers alkane bacterial protein gold hydrogenase immobilized protein nickel iron hydrogenase nickel-iron hydrogenase proton thiol derivative adsorption article chemistry Desulfovibrio gigas Desulfovibrio vulgaris electrode enzymology kinetics molecular dynamics pH thermodynamics Adsorption Alkanes Bacterial Proteins Desulfovibrio gigas Desulfovibrio vulgaris Electrodes Gold Hydrogen-Ion Concentration Hydrogenase Immobilized Proteins Kinetics Molecular Dynamics Simulation Protons Sulfhydryl Compounds Thermodynamics |
| description |
Understanding the interaction and immobilization of [NiFe] hydrogenases on functionalized surfaces is important in the field of biotechnology and, in particular, for the development of biofuel cells. In this study, we investigated the adsorption behavior of the standard [NiFe] hydrogenase of Desulfovibrio gigas on amino-terminated alkanethiol self-assembled monolayers (SAMs) with different levels of protonation. Classical all-atom molecular dynamics (MD) simulations revealed a strong correlation between the adsorption behavior and the level of ionization of the chemically modified electrode surface. While the hydrogenase undergoes a weak but stable initial adsorption process on SAMs with a low degree of protonation, a stronger immobilization is observable on highly ionized SAMs, affecting protein reorientation and conformation. These results were validated by complementary surface-enhanced infrared absorption (SEIRA) measurements on the comparable [NiFe] standard hydrogenases from Desulfovibrio vulgaris Miyazaki F and allowed in this way for a detailed insight into the adsorption mechanism at the atomic level. © 2012 American Chemical Society. |
| author |
Castro, Maria Ana |
| author_facet |
Castro, Maria Ana |
| author_sort |
Castro, Maria Ana |
| title |
Effect of the protonation degree of a self-assembled monolayer on the immobilization dynamics of a [NiFe] hydrogenase |
| title_short |
Effect of the protonation degree of a self-assembled monolayer on the immobilization dynamics of a [NiFe] hydrogenase |
| title_full |
Effect of the protonation degree of a self-assembled monolayer on the immobilization dynamics of a [NiFe] hydrogenase |
| title_fullStr |
Effect of the protonation degree of a self-assembled monolayer on the immobilization dynamics of a [NiFe] hydrogenase |
| title_full_unstemmed |
Effect of the protonation degree of a self-assembled monolayer on the immobilization dynamics of a [NiFe] hydrogenase |
| title_sort |
effect of the protonation degree of a self-assembled monolayer on the immobilization dynamics of a [nife] hydrogenase |
| publishDate |
2013 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_07437463_v29_n2_p673_Utesch http://hdl.handle.net/20.500.12110/paper_07437463_v29_n2_p673_Utesch |
| work_keys_str_mv |
AT castromariaana effectoftheprotonationdegreeofaselfassembledmonolayerontheimmobilizationdynamicsofanifehydrogenase |
| _version_ |
1768545055800295424 |