Zobrazeno 1 - 10
of 158
pro vyhledávání: '"John H. Richards"'
Autor:
Luet-L. Wong, Jorge L. Colón, Danilo R. Casimiro, Jay R. Winkler, I-Jy Chang, John H. Richards, Thomas E. Zewert, Harry B. Gray
Site-directed mutants of human myoglobin have been prepared and characterized; each protein has a single surface-modifiable histidine (at position 48, 70, or 83). The proteins were modified by covalent attachment of pentaammineruthenium (a_5Ru) to th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0a98c620a22357fde409664a5dad41c7
https://ora.ox.ac.uk/objects/uuid:7679a33d-e4da-456f-9aab-20ae73510e44
https://ora.ox.ac.uk/objects/uuid:7679a33d-e4da-456f-9aab-20ae73510e44
Publikováno v:
Journal of Inorganic Biochemistry. 115:119-126
Blue copper proteins (BCPs) comprise classic cases of Nature's profound control over the electronic structures and chemical reactivity of transition metal ions. Early studies of BCPs focused on their inner coordination spheres, that is, residues that
Autor:
Alejandro J. Vila, Kyle M. Lancaster, Frank Neese, Mahesh Sundararajan, Harry B. Gray, Stephen Sproules, Serena DeBeer, John H. Richards, María-Eugenia Zaballa
Publikováno v:
Journal of the American Chemical Society. 134:8241-8253
Bioinorganic canon states that active-site thiolate coordination promotes rapid electron transfer (ET) to and from type 1 copper proteins. In recent work, we have found that copper ET sites in proteins also can be constructed without thiolate ligatio
Autor:
John H. Richards, Scot Wherland, Israel Pecht, Edward J. Crane, Ole Farver, Kyle M. Lancaster, Harry B. Gray
Publikováno v:
Journal of the American Chemical Society. 133:4865-4873
Type zero copper is a hard-ligand analogue of the classical type 1 or blue site in copper proteins that function as electron transfer (ET) agents in photosynthesis and other biological processes. The EPR spectroscopic features of type zero Cu^(II) ar
Publikováno v:
Nature chemistry
Many proteins contain copper in a range of coordination environments, where it has various biological roles, such as transferring electrons or activating dioxygen. These copper sites can be classified by their function or spectroscopic properties. Th
Publikováno v:
Review of Policy Research. 26:105-125
How did political economy help shape the revolution in telecommunications and computer networking? We offer three arguments concerning the impact of political economy and policy on the architecture of the U.S. information and communication technology
Autor:
Pavel Matousek, Michael Towrie, Antonín Vlček, John H. Richards, Cristian Grǎdinaru, Brian R. Crane, Ana María Blanco-Rodríguez, Brian S. Leigh, Michael Busby, Angel J. Di Bilio, Harry B. Gray
Publikováno v:
Journal of the American Chemical Society. 128:4365-4370
The triplet metal-to-ligand charge transfer (3MLCT) dynamics of two structurally characterized ReI(CO)3(phen)(HisX)-modified (phen = 1,10-phenanthroline; X = 83, 109) Pseudomonas aeruginosa azurins have been investigated by picosecond time-resolved i
Autor:
Harry B. Gray, John H. Richards, Michele A. McGuirl, Chalita Thanyakoop, Jay R. Winkler, Jennifer C. Lee, Julia G. Lyubovitsky
Publikováno v:
Biochimica et Biophysica Acta (BBA) - General Subjects. 1619:23-28
The cytochrome (cyt) c', cyt c(556), and cyt c(2) genes from Rhodopseudomonas palustris have been cloned; recombinant cyt c' and cyt c(556) have been expressed, purified, and characterized. Unlike mitochondrial cyt c, these two proteins are structura
Publikováno v:
Journal of Inorganic Biochemistry. 88:375-380
In azurins and other blue copper proteins with relatively low reduction potentials (E(0) [Cu(II)/Cu(I)]400 mV vs. normal hydrogen electrode), the folded polypeptide framework constrains both copper(II) and copper(I) in such a way as to tune the reduc
Autor:
Cynthia N. Kiser, Glen R. Loppnow, Harry B. Gray, Jay R. Winkler, Angel J. Di Bilio, M. Adam Webb, John H. Richards
Publikováno v:
The Journal of Physical Chemistry B. 104:10915-10920
The resonance Raman spectra for Pseudomonas aeruginosa Met121Glu azurin have been measured at wavelengths throughout the 600-nm absorption band at low and high pH. The spectra of the mutant at pH 3.5 and 7.0 are identical. Analysis of the 600-nm abso