Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Bruce R. Lichtenstein"'
Autor:
Matilda Clark, Konstantinos Tornesakis, Gerhard König, Michael Zahn, Bruce R. Lichtenstein, Andrew R. Pickford, Paul A. Cox
Publikováno v:
ACS Omega, Vol 9, Iss 44, Pp 44724-44733 (2024)
Externí odkaz:
https://doaj.org/article/e2cf4f265a954314a9f465e3c574cecd
Autor:
Luisana Avilan, Bruce R. Lichtenstein, Gerhard König, Michael Zahn, Mark D. Allen, Liliana Oliveira, Matilda Clark, Victoria Bemmer, Rosie Graham, Harry P. Austin, Graham Dominick, Christopher W. Johnson, Gregg T. Beckham, John E. McGeehan, Andrew R. Pickford
Publikováno v:
ChemSusChem. 16
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6d53e152bc743b56b2fd328c99ec79c1
https://doi.org/10.1002/cssc.202300472
https://doi.org/10.1002/cssc.202300472
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::72e761ce56ab1670f44ebc0eccb3e837
https://doi.org/10.1042/bst20120067
https://doi.org/10.1042/bst20120067
Autor:
P. Leslie Dutton, Bruce R. Lichtenstein, Christopher C. Moser, Bryan A. Fry, Chris Bialas, Jose F. Cerda
Publikováno v:
Angewandte Chemie (International ed. in English). 54(46)
The first principles design of manmade redox-protein maquettes is used to clarify the physical/chemical engineering supporting the mechanisms of natural enzymes with a view to recapitulate and surpass natural performance. Herein, we use intein-based
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9147b60237ec0dc26d0536778958c422
https://pubmed.ncbi.nlm.nih.gov/26366882
https://pubmed.ncbi.nlm.nih.gov/26366882
Publikováno v:
Tetrahedron Letters. 53:1201-1203
Safranines hold great promise as artificial flavin-like electron transfer cofactors with tunable properties. We report the design and chemical synthesis of the p-methoxy derivative of safranine O using a new synthetic route based on the Ulmann conden
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::441885adf2f05a8268cf5fa4848e807c
https://doi.org/10.1016/j.tetlet.2011.12.028
https://doi.org/10.1016/j.tetlet.2011.12.028
Autor:
Jessica A Siedlecki, P. Leslie Dutton, Kathleen G. Valentine, J. L. Ross Anderson, Chris Bialas, Bruce R. Lichtenstein, Matthew A. Stetz, Lee A. Solomon, Nathan M. Ennist, Zhenyu Zhao, Goutham Kodali, Tammer A. Farid, Bryan A. Fry, A. Joshua Wand, Bohdana M. Discher, Christopher C. Moser, Molly M. Sheehan
Emulating functions of natural enzymes in man-made constructs has proven challenging. Here we describe a man-made protein platform that reproduces many of the diverse functions of natural oxidoreductases without importing the complex and obscure inte
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bc6d600fa623007b0635d84655d80074
https://europepmc.org/articles/PMC4034760/
https://europepmc.org/articles/PMC4034760/
As a prelude to engineering artificial energy conversion proteins emulating biology, we examine the inclusion of a synthetic naphthoquinone amino acid in a characterized host–guest protein and determine the effects of its quinone and hydroquinone f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::266d3c9496e67979e9e494eeb012fd21
https://europepmc.org/articles/PMC3547611/
https://europepmc.org/articles/PMC3547611/
Publikováno v:
ChemInform. 40
The synthesis of a naphthoquinone amino acid and its electrochemical characterization in a peptide is presented.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::951bbedea5c85d9daee64000e31c7f53
https://doi.org/10.1002/chin.200921185
https://doi.org/10.1002/chin.200921185
Publikováno v:
Chemical communications (Cambridge, England). (2)
The synthesis of a naphthoquinone amino acid and its electrochemical characterization in a peptide is presented.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2802740b5b68002cee201aadb0649d20
https://pubmed.ncbi.nlm.nih.gov/19099057
https://pubmed.ncbi.nlm.nih.gov/19099057
Autor:
Jose F. Cerda, Ronald L. Koder, Anne-Frances Miller, Christopher M. Moser, Bruce R. Lichtenstein, P. Leslie Dutton
We report a simple, single step reaction that transforms riboflavin, which is insoluble in benzene, to tetraphenylacetyl riboflavin (TPARF), which is soluble in this solvent to over 250 mM. Electrochemical analysis of TPARF both alone and in complexe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f1db7e57552199b279dff56266f4d49a
https://europepmc.org/articles/PMC3553856/
https://europepmc.org/articles/PMC3553856/