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1.
J Nanosci Nanotechnol ; 21(4): 2342-2350, 2021 04 01.
Article in English | MEDLINE | ID: mdl-33500050

ABSTRACT

Photosynthetic reaction center proteins (RC) purified from purple bacterial strains were deposited on graphene layer prepared by liquid phase exfoliation and light-induced resistance change was measured. By measuring the temperature dependence of the resistance change of the bare and RC covered graphene and comparing with the one inactivated by protein unfolding, two effects were possible to separate. One of them is the resistance change due to temperature effect. The other one clearly indicates a possible electric/electronic interaction between the charge flow in the graphene and the light-induced charge pair within the protein, which is, essentially, different in the open (dark, PBPheo) and closed (light, P+BPheo-) states. These results provide useful information for designing hybrid bio-photonic devices which are able to absorb and convert light energy.

2.
Photosynth Res ; 132(2): 127-134, 2017 May.
Article in English | MEDLINE | ID: mdl-27709414

ABSTRACT

Specific inhibitory reactions of herbicides with photosynthetic reaction centers bound to working electrodes were monitored in a conventional electrochemical cell and a newly designed microfluidic electrochemical flow cell. In both cases, the bacterial reaction centers were bound to a transparent conductive metal oxide, indium-tin-oxide, electrode through carbon nanotubes. In the conventional cell, photocurrent densities of up to a few µA/cm2 could be measured routinely. The photocurrent could be blocked by the photosynthetic inhibitor terbutryn (I 50 = 0.38 ± 0.14 µM) and o-phenanthroline (I 50 = 63.9 ± 12.2 µM). The microfluidic flow cell device enabled us to reduce the sample volume and to simplify the electrode arrangement. The useful area of the electrodes remained the same (ca. 2 cm2), similar to the classical electrochemical cell; however, the size of the cell was reduced considerably. The microfluidic flow control enabled us monitoring in real time the binding/unbinding of the inhibitor and cofactor molecules at the secondary quinone site.


Subject(s)
Biosensing Techniques/methods , Electrochemistry/instrumentation , Herbicides , Photosynthesis/physiology
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