Coupled Electron/Proton Transfer in Complex Flavoproteins
نویسندگان
چکیده
منابع مشابه
Coupled coincidence point and common coupled fixed point theorems in complex valued metric spaces
In this paper, we introduce the concept of a w-compatible mappings and utilize the same to discuss the ideas of coupled coincidence point and coupled point of coincidence for nonlinear contractive mappings in the context of complex valued metric spaces besides proving existence theorems which are following by corresponding unique coupled common fixed point theorems for such mappings. Some illus...
متن کاملEPR on Flavoproteins.
Flavoproteins often employ radical mechanisms in their enzymatic reactions. This involves paramagnetic species, which can ideally be investigated with electron paramagnetic resonance (EPR) spectroscopy. In this chapter we focus on the example of flavin-based photoreceptors and discuss, how different EPR methods have been used to extract information about the flavin radical's electronic state, i...
متن کاملA mononuclear ruthenium complex showing multiple proton-coupled electron transfer toward multi-electron transfer reactions.
Two new ruthenium(II) complexes bearing dissociable protons, [Ru(trpy)(H(2)bim)Cl]PF(6) (1) and [Ru(trpy)(H(2)bim)(OH(2))](PF(6))(2) (2) (H(2)bim = 2,2'-biimidazole and trpy = 2,2':6',2''-terpyridine), were synthesized and characterized, where the H(2)bim and M-OH(2) moieties are expected to serve as proton-dissociation sites. Single crystal X-ray diffraction analyses revealed that the H(2)bim ...
متن کاملProton-coupled electron transfer.
Proton-coupled electron transfer (PCET) is an important mechanism for charge transfer in a wide variety of systems including biology- and materials-oriented venues. We review several areas where the transfer of an electron and proton is tightly coupled and discuss model systems that can provide an experimental basis for a test of PCET theory. In a PCET reaction, the electron and proton may tran...
متن کاملActive-site probes of flavoproteins.
The chemical reactivity of 8-chloroflavins and 8-mercaptoflavins has been exploited in order to examine the orientation of protein-bound flavins relative to solvent. The apoprotein form of a series of flavoproteins was prepared and the native flavin was replaced by either 8-C1-flavin or 8-mercaptoflavin (FAD, FMN, or riboflavin form as was appropriate). The reconstituted proteins were exposed t...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2001
ISSN: 0021-9258
DOI: 10.1074/jbc.m100673200