Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Sarah E Chobot"'
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:
Sarah E. Chobot, Bryan A. Fry, P. Leslie Dutton, Christopher C. Moser, Gregory Wiedman, Bohdana M. Discher, Geetha Goparaju
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1857(5):503-512
Here we describe the design, Escherichia coli expression and characterization of a simplified, adaptable and functionally transparent single chain 4-α-helix transmembrane protein frame that binds multiple heme and light activatable porphyrins. Such
Autor:
Zhenyu Zhao, David Snell, Christopher C. Moser, Bruce R. Lichtenstein, Lee A. Solomon, Sarah E. Chobot, J. L. Ross Anderson, Chris Bialas, Sergei A. Vinogradov, Tatiana V. Esipova, Goutham Kodali, Joshua A. Mancini, Bryan A. Fry, Bohdana M. Discher, Tammer A. Farid, Nathan M. Ennist, P. Leslie Dutton, Craig T. Armstrong, Molly M. Sheehan
Publikováno v:
Biochemical Society Transactions. 40:561-566
The study of natural enzymes is complicated by the fact that only the most recent evolutionary progression can be observed. In particular, natural oxidoreductases stand out as profoundly complex proteins in which the molecular roots of function, stru
Publikováno v:
Biochemistry
Thioredoxin reductases (TrxRs) are flavin-containing dithioloxidoreductases that couple reduction equivalents from the soluble NAD(P)H pool to the soluble protein thioredoxin (Trx). Previous crystallographic studies of the Escherichia coli enzyme ( e
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1777(7-8):1032-1037
There is no doubt that distance is the principal parameter that sets the order of magnitude for electron-tunneling rates in proteins. However, there continue to be varying ways to measure electron-tunneling distances in proteins. This distance uncert
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:
Sarah E. Chobot, James J. Collins, Erin L. Eastwood, Sean Elliott, Scott E. Schaus, Andrew P. Wojtovich, Diego di Bernardo, Timothy S. Gardner, Michael Thompson
Publikováno v:
Nature Biotechnology. 23:377-383
A major challenge in drug discovery is to distinguish the molecular targets of a bioactive compound from the hundreds to thousands of additional gene products that respond indirectly to changes in the activity of the targets1,2,3,4,5,6,7,8. Here, we
Autor:
Richard B. Silverman, Sarah E. Chobot, Brian R. Crane, Kristin J. Labby, Dmitriy Lukoyanov, Roman Davydov, Brian M. Hoffman
Publikováno v:
Biochemistry
Nitric oxide synthase (NOS) catalyzes the conversion of L-arginine to L-citrulline and NO in a two-step process involving the intermediate N(ω)-hydroxy-L-arginine (NHA). It was shown that Cpd I is the oxygenating species for L-arginine; the hydroper
Publikováno v:
Angewandte Chemie. 119:4223-4225
Publikováno v:
Journal of bioenergetics and biomembranes. 40(5)
Thirty years ago, Peter Mitchell won the Nobel Prize for proposing how electrical and proton gradients across bioenergetic membranes were the energy coupling intermediate between photosynthetic and respiratory electron transfer and cellular activitie