Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Terrence E. Meyer"'
Autor:
Terrence E. Meyer, Joann Sanders-Loehr, Gabriele Backes, William V. Sweeney, Yoshiki Mino, Thomas M. Loehr, Michael A. Cusanovich, Elinor T. Adman
Publikováno v:
Journal of the American Chemical Society. 113:2055-2064
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7dfb4581e995e834fac15e98ad05a5c6
https://doi.org/10.1021/ja00006a027
https://doi.org/10.1021/ja00006a027
Autor:
Terrence E. Meyer, David P. Millar, Tammy T. Woo, Ronald Brudler, G. Tollin, Elizabeth D. Getzoff, Ulrich K. Genick, Savitha Devanathan, Klaus Gerwert, Michael A. Cusanovich
Publikováno v:
Biochemistry. 39(44)
To understand in atomic detail how a chromophore and a protein interact to sense light and send a biological signal, we are characterizing photoactive yellow protein (PYP), a water-soluble, 14 kDa blue-light receptor which undergoes a photocycle upon
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aae6506a866c22be4451acbb90dcb19c
https://pubmed.ncbi.nlm.nih.gov/11063584
https://pubmed.ncbi.nlm.nih.gov/11063584
Autor:
James A. Fuchs, José A. Navarro, Florence K. Gleason, Michael A. Cusanovich, Gordon Tollin, Terrence E. Meyer
Publikováno v:
Biochemistry. 30(8)
The reduction of Escherichia coli thioredoxin by thioredoxin reductase was studied by stopped-flow spectrophotometry. The reaction showed no dependence on thioredoxin concentration, indicating that complex formation was rapid and occurred during the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ecbebc1779d58670f359ea29273af11e
https://pubmed.ncbi.nlm.nih.gov/1998679
https://pubmed.ncbi.nlm.nih.gov/1998679
Publikováno v:
Biochimica et biophysica acta. 1076(1)
Cyanide binding to Chromatium vinosum ferricytochrome c' has been studied to further investigate possible allosteric interactions between the subunits of this dimeric protein. Cyanide binding to C. vinosum cytochrome c' appears to be cooperative. How
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dc2c75cf87f33f55f5759d62a9a7c0fc
https://pubmed.ncbi.nlm.nih.gov/1846081
https://pubmed.ncbi.nlm.nih.gov/1846081
Publikováno v:
Biochemistry. 29(7)
The kinetics of the reversible binding of cyanide by the ferric cytochrome c' from Chromatium vinosum have been studied over the pH range 6.9-9.6. The reaction is extremely slow at neutral pH compared to the reactions of other high-spin ferric heme p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fb918be87c44d0a8f4eee5e4253492f3
https://pubmed.ncbi.nlm.nih.gov/2158816
https://pubmed.ncbi.nlm.nih.gov/2158816
Publikováno v:
Biochemistry. 28:2140-2144
Equilibrium constants for the binding of a series of alkyl isocyanides to ferrous cytochrome c' from Rhodospirillum molischianum have been measured spectrophotometrically. The equilibrium constants range from 3.3 M-1 to 2.6 x 10(2) M-1 and follow the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::398a6d89ec0f20501c631184ba1abcb0
https://doi.org/10.1021/bi00431a027
https://doi.org/10.1021/bi00431a027
Publikováno v:
European journal of biochemistry. 181(1)
The high-potential iron-sulfur protein (HiPIP) from Rhodospirillum tenue (strain 3761) shows only a weak (20-25%) sequence similarity to HiPIPs from Chromatium vinosum, Ectothiorhodospira halophila and Ectothiorhodospira vacuolata, including the stri
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cb27d4ae1f71676e68a62653b4e3f2dc
https://pubmed.ncbi.nlm.nih.gov/2714284
https://pubmed.ncbi.nlm.nih.gov/2714284
Publikováno v:
Biochemistry. 26(25)
The thermodynamic parameters for carbon binding to monomeric Rhodopseudomonas palustris cytochrome c' are determined. An enthalpy change for CO(aq) binding to the cytochrome is measured directly by titration calorimetry as -6.7 +/- 0.2 kcal/mol of he
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e1724023c268f8403f59d20ff11b4906
https://pubmed.ncbi.nlm.nih.gov/2831936
https://pubmed.ncbi.nlm.nih.gov/2831936