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 Desulf...

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Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1992. - 29(2013), 2 vom: 15. Jan., Seite 673-82
1. Verfasser: Utesch, Tillmann (VerfasserIn)
Weitere Verfasser: Millo, Diego, Castro, Maria Ana, Hildebrandt, Peter, Zebger, Ingo, Mroginski, Maria Andrea
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2013
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Alkanes Bacterial Proteins Immobilized Proteins Protons Sulfhydryl Compounds Gold 7440-57-5 nickel-iron hydrogenase mehr... EC 1.12.- Hydrogenase EC 1.12.7.2
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520 |a 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 
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650 4 |a Research Support, Non-U.S. Gov't 
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650 7 |a Bacterial Proteins  |2 NLM 
650 7 |a Immobilized Proteins  |2 NLM 
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650 7 |a 7440-57-5  |2 NLM 
650 7 |a nickel-iron hydrogenase  |2 NLM 
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650 7 |a Hydrogenase  |2 NLM 
650 7 |a EC 1.12.7.2  |2 NLM 
700 1 |a Millo, Diego  |e verfasserin  |4 aut 
700 1 |a Castro, Maria Ana  |e verfasserin  |4 aut 
700 1 |a Hildebrandt, Peter  |e verfasserin  |4 aut 
700 1 |a Zebger, Ingo  |e verfasserin  |4 aut 
700 1 |a Mroginski, Maria Andrea  |e verfasserin  |4 aut 
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