Zobrazeno 1 - 10
of 109
pro vyhledávání: '"and Melvin Y. Okamura"'
Publikováno v:
Photosynthesis Research. 137:361-375
We provide a tribute to George Feher, one of the founding scientists in the use of biophysical techniques to probe photosynthetic complexes, especially the bacterial reaction center. His early life is briefly reviewed followed by a description of the
Publikováno v:
Biochemistry. 47:13318-13325
The role of short-range hydrogen bond interactions at the interface between electron transfer proteins cytochrome c(2) (cyt) and the reaction center (RC) from Rhodobacter sphaeroides was studied by mutation (to Ala) of RC residues Asn M187, Asn M188,
Publikováno v:
Biochemistry. 46:8234-8243
Proton ENDOR spectroscopy was used to monitor local conformational changes in bacterial reaction centers (RC) associated with the electron transfer reaction DQB → D+•QB−• using mutant RCs capable of photo-reducing QB at cryogenic temperatures
Publikováno v:
Biochemistry. 46:1176-1182
In the photosynthetic reaction center (RC) from the purple bacterium Rhodobacter sphaeroides, proton-coupled electron-transfer reactions occur at the secondary quinone (QB) site. Involved in the proton uptake steps are carboxylic acids, which have ch
Publikováno v:
Biochemistry. 44:14519-14527
In the photosynthetic reaction center (RC) from the purple bacterium Rhodobacter sphaeroides, proton-coupled electron-transfer reactions occur at the secondary quinone (Q(B)) site. Several nearby residues are important for both binding and redox chem
Autor:
Melvin Y. Okamura, Herbert L. Axelrod
Publikováno v:
Photosynthesis Research. 85:101-114
In the photosynthetic bacterium, Rhodobacter sphaeroides, the mobile electron carrier, cytochrome c2 (cyt c2) transfers an electron from reduced heme to the photooxidized bacteriochlorophyll dimer in the membrane bound reaction center (RC) as part of
Publikováno v:
Biochemistry. 44:9619-9625
The cation-pi interaction between positively charged and aromatic groups is a common feature of many proteins and protein complexes. The structure of the complex between cytochrome c(2) (cyt c(2)) and the photosynthetic reaction center (RC) from Rhod
Autor:
E. C. Abresch, Q. Xu, C. Chang, George Feher, Herbert L. Axelrod, Mark L. Paddock, Melvin Y. Okamura
Publikováno v:
Biochemistry. 44:6920-6928
The photosynthetic reaction center (RC) from purple bacteria converts light into chemical energy. Although the RC shows two nearly structurally symmetric branches, A and B, light-induced electron transfer in the native RC occurs almost exclusively al
Publikováno v:
Biochemistry. 43:7236-7243
In the reaction center from the photosynthetic purple bacterium Rhodobacter sphaeroides, light energy is rapidly converted to chemical energy through coupled electron-proton transfer to a buried quinone molecule Q(B). Involved in the proton uptake st
Autor:
Qiang Xu, George Feher, Melvin Y. Okamura, E. C. Abresch, Herbert L. Axelrod, Mark L. Paddock
Publikováno v:
Structure. 12:703-715
In the photosynthetic reaction center (RC) from Rhodobacter sphaeroides , the reduction of a bound quinone molecule Q B is coupled with proton uptake. When Asp-L213 is replaced by Asn, proton transfer is inhibited. Proton transfer was restored by two