Zobrazeno 1 - 10
of 148
pro vyhledávání: '"Bridgette A Barry"'
Publikováno v:
PLoS ONE, Vol 7, Iss 7, p e42220 (2012)
Light stress in plants results in damage to the water oxidizing reaction center, photosystem II (PSII). Redox signaling, through oxidative modification of amino acid side chains, has been proposed to participate in this process, but the oxidative sig
Externí odkaz:
https://doaj.org/article/1299025b23a84e94a90a9dcfa26e0c79
Autor:
R. Atlee Watson, Bridgette A. Barry, Adam R. Offenbacher, Raquel L. Lieberman, Mohammad S. Safiarian
Publikováno v:
The Journal of Physical Chemistry Letters. 12:9020-9025
Ribonucleotide reductase (RNR), which supplies the building blocks for DNA biosynthesis and its repair, has been linked to human diseases and is emerging as a therapeutic target. Here, we present a mechanistic investigation of triapine (3AP), a clini
Publikováno v:
The journal of physical chemistry. B. 125(30)
The enzyme, ribonucleotide reductase (RNR), is essential for DNA synthesis in all cells. The class Ia Escherichia coli RNR consists of two dimeric subunits, α2 and β2, which form an active but unstable heterodimer of dimers, α2β2. The structure o
Autor:
San Hui Chi, James C. Gumbart, Miranda McDaniel, Zhanjun Guo, Hyea Hwang, Bridgette A. Barry, Tyler G. McCaslin, Cynthia V. Pagba, Joseph W. Perry, Cristina Olivieri, Gianluigi Veglia, Fernando Porcelli
Publikováno v:
The Journal of Physical Chemistry. B
Tyrosine–tryptophan (YW) dyads are ubiquitous structural motifs in enzymes and play roles in proton-coupled electron transfer (PCET) and, possibly, protection from oxidative stress. Here, we describe the function of YW dyads in de novo designed 18-
Autor:
Tyler G. McCaslin, Joseph W. Perry, Bridgette A. Barry, James C. Gumbart, Cynthia V. Pagba, Hyea Hwang, San-Hui Chi
Publikováno v:
Chemical Communications. 55:9399-9402
Tyrosine residues act as intermediates in proton coupled electron transfer reactions (PCET) in proteins. For example, in ribonucleotide reductase (RNR), a tyrosyl radical oxidizes an active site cysteine via a 35 A pathway that contains multiple arom
Publikováno v:
The journal of physical chemistry. B. 124(2)
Proton-coupled electron transfer (PCET) is fundamental to many important biological reactions, including solar energy conversion and DNA synthesis. For example, class Ia ribonucleotide reductases (RNRs) contain a tyrosyl radical-diiron cofactor with
Publikováno v:
ChemPhysChem. 19:1428-1431
As a noninvasive molecular analysis technique, ultraviolet resonance Raman (UVRR) spectroscopy represents a label-free method suitable for characterizing biomolecules. Using UVRR spectroscopy, we collected spectral fingerprints of UV absorbing cellul
Chloride Maintains a Protonated Internal Water Network in the Photosynthetic Oxygen Evolving Complex
Publikováno v:
The Journal of Physical Chemistry B. 121:10327-10337
In photosystem II (PSII), water oxidation occurs at a Mn4CaO5 cluster and results in production of molecular oxygen. The Mn4CaO5 cluster cycles among five oxidation states, called Sn states. As a result, protons are released at the metal cluster and
Autor:
Bridgette A. Barry, Zhanjun Guo
Publikováno v:
The Journal of Physical Chemistry B. 121:3987-3996
A redox-active tyrosine, YZ (Y161 in the D1 polypeptide), is essential in photosystem II (PSII), which conducts photosynthetic oxygen evolution. On each step of the light-driven oxygen evolving reaction, YZ radical is formed by a chlorophyll cation r
Autor:
Bridgette A. Barry, Tyler G. McCaslin, James C. Gumbart, Hyea Hwang, Cynthia V. Pagba, Christina M. Nevin, Anna Pavlova, Anthony Hazel
Publikováno v:
The Journal of Physical Chemistry B. 121:3536-3545
Tyrosine-based radical transfer plays an important role in photosynthesis, respiration, and DNA synthesis. Radical transfer can occur either by electron transfer (ET) or proton coupled electron transfer (PCET), depending on the pH. Reversible conform