cytochrome-c-t has been researched along with triethanolamine* in 1 studies
1 other study(ies) available for cytochrome-c-t and triethanolamine
| Article | Year |
|---|---|
Photoactivation studies of zinc porphyrin-myoglobin system and its application for light-chemical energy conversion.
An artificial zinc porphyrin-myoglobin-based photo-chemical energy conversion system, consisting of ZnPP-Mb or ZnPE(1)-Mb as a photosensitizer, NADP(+) as an electron acceptor, and triethanolamine as an electron donor, has been constructed to mimic photosystem I. The photoirradiated product is able to reduce a single-electron acceptor protein cytochrome c, but cannot catalyze the two-electron reduction of acetaldehyde by alcohol dehydrogenase, thus demonstrating a single electron transfer mechanism. Furthermore, the artificial system can bifunctionally promote oxidoredox reactions, depending on the presence or absence of a sacrificial electron donor, thus suggesting its potential application in electrochemical regeneration steps involved in chemical transformation and/or energy conversion. Topics: Cytochromes c; Ethanolamines; Fluorescence Polarization; Metalloporphyrins; Models, Chemical; Molecular Structure; Myoglobin; NADP; Oxidation-Reduction; Photochemical Processes; Photosensitizing Agents; Photosynthesis | 2011 |