Zobrazeno 1 - 10
of 27
pro vyhledávání: '"Jennifer K. Schwartz"'
Autor:
Edward I. Solomon, Takehiko Tosha, Elizabeth C. Theil, Jennifer K. Schwartz, Yeonju Kwak, Suranjana Haldar, Rabindra K. Behera
Publikováno v:
Biochemistry
Ferritin has a binuclear non-heme iron active site that functions to oxidize iron as a substrate for formation of an iron mineral core. Other enzymes of this class have tightly bound diiron cofactor sites that activate O2 to react with substrate. Fer
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e7eb9b59f80cdfd8fdd6b58af1d2a688
https://doi.org/10.1021/bi4013726
https://doi.org/10.1021/bi4013726
Autor:
Yeonju Kwak, Martin Srnec, Jennifer K. Schwartz, Lubomír Rulíšek, Edward I. Solomon, Tibor András Rokob
Publikováno v:
Inorganic Chemistry. 51:2806-2820
Large-scale quantum and molecular mechanical methods (QM/MM) and QM calculations were carried out on the soluble Δ(9) desaturase (Δ(9)D) to investigate various structural models of the spectroscopically defined peroxodiferric (P) intermediate. This
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5e5711dded100f7d3a47da2091ae62de
https://doi.org/10.1021/ic2018067
https://doi.org/10.1021/ic2018067
Publikováno v:
Journal of Chemical Information and Modeling. 51:2164-2173
A Genetic Algorithm (GA) is a stochastic optimization technique based on the mechanisms of biological evolution. These algorithms have been successfully applied in many fields to solve a variety of complex nonlinear problems. While they have been use
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::58611e0cfcfc32716cbdd153383bcbee
https://doi.org/10.1021/ci2001296
https://doi.org/10.1021/ci2001296
Publikováno v:
Journal of the American Chemical Society. 130:9441-9450
Maxi ferritins, 24 subunit protein nanocages, are essential in humans, plants, bacteria, and other animals for the concentration and storage of iron as hydrated ferric oxide, while minimizing free radical generation or use by pathogens. Formation of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::41177a4f54d370395469e8afb46a8fac
https://doi.org/10.1021/ja801251q
https://doi.org/10.1021/ja801251q
Autor:
Jennifer K. Schwartz, Victor W. Huang, Yeonju Kwak, Donald M. Kurtz, Edward I. Solomon, Emily Boice
Publikováno v:
Biochemistry. 54(47)
Ferritins and bacterioferritins (Bfrs) utilize a binuclear non-heme iron binding site to catalyze oxidation of Fe(II), leading to formation of an iron mineral core within a protein shell. Unlike ferritins, in which the diiron site binds Fe(II) as a s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4d3ddd81c61a49efa50c12ee86929467
https://pubmed.ncbi.nlm.nih.gov/26551523
https://pubmed.ncbi.nlm.nih.gov/26551523
Autor:
Kannan Muthukumaran, Dewey Holten,§ and, Jennifer K. Schwartz, James R. Diers, Igor V. Sazanovich, Christine Kirmaier, Eve Hindin, David F. Bocian, Robert S. Loewe, Jonathan S. Lindsey
Publikováno v:
The Journal of Physical Chemistry B. 107:3431-3442
A perylene-oxochlorin dyad has been prepared and characterized for potential use as a new light-harvesting motif. The dyad (PMI−ZnO) consists of a perylene-monoimide dye (PMI) joined at the 5-position of a zinc oxochlorin (ZnO) via a diphenylethyne
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f2183d1474f18dde566ceb113a85d18a
https://doi.org/10.1021/jp026941a
https://doi.org/10.1021/jp026941a
Autor:
Dewey Holten, Eve Hindin, Jennifer K. Schwartz, David F. Bocian, Igor V. Sazanovich, Kannan Muthukumaran, Christine Kirmaier, Masahiko Taniguchi, James R. Diers, Jonathan S. Lindsey,‡ and
Publikováno v:
The Journal of Physical Chemistry B. 107:3443-3454
Three perylene-oxochlorin dyads have been prepared and characterized with the goal of identifying charge-injection or molecular-switching motifs for use in molecular photonics. Each dyad consists of a perylene-bis(imide) dye (PDI) joined at the 10-po
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5c26a43a40d93dbe35b06bc6f0f8f054
https://doi.org/10.1021/jp0269423
https://doi.org/10.1021/jp0269423
Autor:
Takehiko Tosha, Jennifer K. Schwartz, Adrienne R. Diebold, Elizabeth C. Theil, Edward I. Solomon, Xiaofeng S. Liu
Publikováno v:
Biochemistry. 49(49)
DNA protection during starvation (Dps) proteins are miniferritins found in bacteria and archaea that provide protection from uncontrolled Fe(II)/O radical chemistry; thus the catalytic sites are targets for antibiotics against pathogens, such as anth
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::706a7fe330927badc0a0ad74d4f33b08
https://pubmed.ncbi.nlm.nih.gov/21028901
https://pubmed.ncbi.nlm.nih.gov/21028901
Autor:
Eve Hindin, Robert R. Birge, Fabien Chevalier, Jennifer K. Schwartz, Christine Kirmaier, David F. Bocian, Jonathan S. Lindsey, Hee-eun Song, Lavoisier Ramos, Robert S. Loewe, Eunkyung Yang, Kin-ya Tomizaki, Dewey Holten, James R. Diers
Publikováno v:
The journal of physical chemistry. B. 114(45)
Seven perylene-porphyrin dyads were examined with the goal of identifying those most suitable for components of light-harvesting systems. The ideal dyad should exhibit strong absorption by the perylene in the green, undergo rapid and efficient excite
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e948ece10d50689c56f9458250b499d0
https://pubmed.ncbi.nlm.nih.gov/20112987
https://pubmed.ncbi.nlm.nih.gov/20112987
Publikováno v:
Biochemistry. 47(32)
The multicomponent soluble form of methane monooxygenase (sMMO) catalyzes the oxidation of methane through the activation of O 2 at a nonheme biferrous center in the hydroxylase component, MMOH. Reactivity is limited without binding of the sMMO effec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e1e0ff4b5d9624d3aa526c36880af12d
https://pubmed.ncbi.nlm.nih.gov/18627173
https://pubmed.ncbi.nlm.nih.gov/18627173