منابع مشابه
Protein electron transfer: is biology (thermo)dynamic?
Simple physical mechanisms are behind the flow of energy in all forms of life. Energy comes to living systems through electrons occupying high-energy states, either from food (respiratory chains) or from light (photosynthesis). This energy is transformed into the cross-membrane proton-motive force that eventually drives all biochemistry of the cell. Life's ability to transfer electrons over lar...
متن کاملProtein electron transfer: Dynamics and statistics.
Electron transfer between redox proteins participating in energy chains of biology is required to proceed with high energetic efficiency, minimizing losses of redox energy to heat. Within the standard models of electron transfer, this requirement, combined with the need for unidirectional (preferably activationless) transitions, is translated into the need to minimize the reorganization energy ...
متن کاملPeptide and protein quantification using iTRAQ with electron transfer dissociation.
Electron transfer dissociation (ETD) has become increasingly used in proteomic analyses due to its complementarity to collision-activated dissociation (CAD) and its ability to sequence peptides with post-translation modifications (PTMs). It was previously unknown, however, whether ETD would be compatible with a commonly employed quantification technique, isobaric tags for relative and absolute ...
متن کاملPicosecond electron transfer from photosynthetic reaction center protein to GaAs.
An extremely fast electron transfer through an electronically coupled junction between covalently bound oriented photosynthetic reaction center protein photosystem I (PS I) and n-GaAs was measured by time-resolved photoluminescence. It was found that the n-GaAs band edge luminescence intensity increased by a factor of 2, and the fast exponential decay constant was increased by a factor of 2.6 f...
متن کاملCoupling coherence distinguishes structure sensitivity in protein electron transfer.
Quantum mechanical analysis of electron tunneling in nine thermally fluctuating cytochrome b562 derivatives reveals two distinct protein-mediated coupling limits. A structure-insensitive regime arises for redox partners coupled through dynamically averaged multiple-coupling pathways (in seven of the nine derivatives) where heme-edge coupling leads to the multiple-pathway regime. A structure-dep...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1996
ISSN: 0014-5793
DOI: 10.1016/0014-5793(97)81275-6