Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Kathryn D Bewley"'
Autor:
Kathryn D Bewley, Mishtu Dey, Rebekah E Bjork, Sangha Mitra, Sarah E Chobot, Catherine L Drennan, Sean J Elliott
Publikováno v:
PLoS ONE, Vol 10, Iss 4, p e0122466 (2015)
Thioredoxins are small soluble proteins that contain a redox-active disulfide (CXXC). These disulfides are tuned to oxidizing or reducing potentials depending on the function of the thioredoxin within the cell. The mechanism by which the potential is
Externí odkaz:
https://doaj.org/article/d99cb6eb7f484f8ca8c18e1e6d537b76
Autor:
Mark A. Burlingame, Joel S. Griffitts, Richard A. Robison, Philip R. Bennallack, Susan M. Miller, Kathryn D. Bewley
Thiopeptides, including micrococcins, are a growing family of bioactive natural products that are ribosomally synthesized and heavily modified. Here we use a refactored, modular in vivo system containing the micrococcin P1 (MP1) biosynthetic genes (T
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::327241661324f51535ba7a2ef70014b2
https://europepmc.org/articles/PMC5098666/
https://europepmc.org/articles/PMC5098666/
Autor:
Sean Elliott, Rebekah E. Bjork, Catherine L. Drennan, Sangha Mitra, Kathryn D. Bewley, Mishtu Dey, Sarah E. Chobot
Publikováno v:
PLoS ONE, Vol 10, Iss 4, p e0122466 (2015)
Public Library of Science
PLoS ONE
Public Library of Science
PLoS ONE
Thioredoxins are small soluble proteins that contain a redox-active disulfide (CXXC). These disulfides are tuned to oxidizing or reducing potentials depending on the function of the thioredoxin within the cell. The mechanism by which the potential is
Autor:
Sean Elliott, Kathryn D. Bewley, Catherine L. Drennan, Nozomi Ando, Mackenzie A. Firer-Sherwood, Jee-Young Mock
Publikováno v:
The FASEB Journal. 27
Autor:
Catherine L. Drennan, Nozomi Ando, Sean Elliott, Kathryn D. Bewley, Jee-Young Mock, Mackenzie A. Firer-Sherwood
Publikováno v:
Prof. Drennan via Erja Kajosalo
Shewanella oneidensis MR-1 has the ability to use many external terminal electron acceptors during anaerobic respiration, such as DMSO. The pathway that facilitates this electron transfer includes the decahaem cytochrome DmsE, a paralogue of the MtrA
Publikováno v:
Metallomics : integrated biometal science. 3(4)
Examining electron transfer between two proteins with identical spectroscopic signatures is a challenging task. It is supposed that several multiheme cytochromes in Shewanella oneidensis form a molecular “wire” through which electrons are transpo
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. (8-9):938-948
While iron is often a limiting nutrient to Biology, when the element is found in the form of heme cofactors (iron protoporphyrin IX), living systems have excelled at modifying and tailoring the chemistry of the metal. In the context of proteins and e