Zobrazeno 1 - 10
of 175
pro vyhledávání: '"and Boi Hanh Huynh"'
Autor:
Attila Szabo, Boi Hanh Huynh, David A. Case, Martin Karplus, Angel Wai-mun Lee, Bruce R. Gelin
Hemoglobin, because of its vital role in oxygen transport and its status as a model for cooperative proteins, has been the subject of a wide range of physical and chemical studies for many years. This chapter presents a brief introduction to the ther
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d60616ab60a25eb51d243241a597a259
https://doi.org/10.1201/9781003068563-2
https://doi.org/10.1201/9781003068563-2
Autor:
Michael K. Johnson, Ricardo Garcia-Serres, Peter Schürmann, Sunil G. Naik, Florence Bourquin, Elizabeth M. Walters, Boi Hanh Huynh, Dominique A. Glauser
Ferredoxin:thioredoxin reductase catalyzes the reduction of thioredoxins in plant chloroplasts using the [Fe2S2] ferredoxin as a one-electron donor and as such plays a central role in light regulation of oxygenic photosynthesis. The active-site compr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6688e455b8aa8448da28b8112698ba2c
http://doc.rero.ch/record/289049/files/Walters_Elizabeth_M._-_Role_of_Histidine-86_in_the_Catalytic_20170630.pdf
http://doc.rero.ch/record/289049/files/Walters_Elizabeth_M._-_Role_of_Histidine-86_in_the_Catalytic_20170630.pdf
Autor:
Guy N. L. Jameson, Michael K. Johnson, Peter Schürmann, Boi Hanh Huynh, Elizabeth M. Walters, Wanda Manieri
Ferredoxin:thioredoxin reductase (FTR) catalyzes the reduction of the disulfide in thioredoxin in two one-electron steps using an active site comprising a [4Fe−4S] in close proximity to a redox active disulfide. Mössbauer spectroscopy has been use
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0f80fe63920117ae04717819f78a0829
http://doc.rero.ch/record/288861/files/Jameson_Guy_N._-_Spectroscopy_Evidence_for_Site_Specific_20170606.pdf
http://doc.rero.ch/record/288861/files/Jameson_Guy_N._-_Spectroscopy_Evidence_for_Site_Specific_20170606.pdf
Publikováno v:
Biochemistry. 51:8071-8084
The mechanism of [4Fe-4S] cluster assembly on A-type Fe-S cluster assembly proteins, in general, and the specific role of (Nif)IscA in the maturation of nitrogen fixation proteins are currently unknown. To address these questions, in vitro spectrosco
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2c70e33d530a31f1466d2e77a9a15c9f
https://doi.org/10.1021/bi3006658
https://doi.org/10.1021/bi3006658
Publikováno v:
Biochemistry. 51:8056-8070
The ability of Azotobacter vinelandii(Nif)IscA to bind Fe has been investigated to assess the role of Fe-bound forms in NIF-specific Fe-S cluster biogenesis. (Nif)IscA is shown to bind one Fe(III) or one Fe(II) per homodimer and the spectroscopic and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6c478f2d4a0bc57f659ee33f7ce5f952
https://doi.org/10.1021/bi300664j
https://doi.org/10.1021/bi300664j
Autor:
Alice S. Pereira, Pedro Tavares, Cristina G. Timóteo, Boi Hanh Huynh, Filipe Folgosa, Márcia Guilherme, Sunil G. Naik, Américo G. Duarte
Publikováno v:
Journal of the American Chemical Society. 134:10822-10832
Ferritins are ubiquitous and can be found in practically all organisms that utilize Fe. They are composed of 24 subunits forming a hollow sphere with an inner cavity of ~80 Å in diameter. The main function of ferritin is to oxidize the cytotoxic Fe(
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d23d497dbab00cd8c81d3b17adc8f225
https://doi.org/10.1021/ja211368u
https://doi.org/10.1021/ja211368u
Autor:
Boi Hanh Huynh, Américo G. Duarte, Alice S. Pereira, Cristina G. Timóteo, Carlos E. Martins, Sunil G. Naik, José J. G. Moura, Pedro Tavares, Isabel Moura
Publikováno v:
Biochemistry. 50:4251-4262
Respiratory nitric oxide reductase (NOR) was purified from membrane extract of Pseudomonas (Ps.) nautica cells to homogeneity as judged by polyacrylamide gel electrophoresis. The purified protein is a heterodimer with subunits of molecular masses of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::180f7fef6758b90521904fa8e3ad5f2a
https://doi.org/10.1021/bi101605p
https://doi.org/10.1021/bi101605p
Autor:
Michael K. Johnson, Daphne T. Mapolelo, Nicholas S. Lees, Sunil G. Naik, Pamela J. Riggs-Gelasco, Haoran Li, Boi Hanh Huynh, Brian M. Hoffman, Caryn E. Outten, Nin N. Dingra
Publikováno v:
Biochemistry. 48:9569-9581
The transcription of iron uptake and storage genes in Saccharomyces cerevisiae is primarily regulated by the transcription factor Aft1. Nucleocytoplasmic shuttling of Aft1 is dependent upon mitochondrial Fe-S cluster biosynthesis via a signaling path
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::724c955abe10f4d32ede43e24f3b1779
https://doi.org/10.1021/bi901182w
https://doi.org/10.1021/bi901182w
Autor:
Maïté Sendra, Sunil G. Naik, Harsimranjit K. Chahal, Marc Fontecave, Boi Hanh Huynh, Vibha Gupta, Sandrine Ollagnier de Choudens, F. Wayne Outten
Publikováno v:
Journal of the American Chemical Society. 131:6149-6153
Iron sulfur (Fe-S) clusters are versatile biological cofactors that require biosynthetic systems in vivo to be assembled. In Escherichia coli the Isc (iscRSUA-hscBA-fdx-iscX) and the Suf (sufABCDSE) pathways fulfill this function. Despite extensive b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a085d9c1dc29321c6b6074734dbaa90e
https://doi.org/10.1021/ja807551e
https://doi.org/10.1021/ja807551e
Autor:
Stephen J. Lippard, Brian M. Hoffman, Sun-Hee Kim, Sunil G. Naik, Roman Davydov, Ricardo Garcia-Serres, Leslie J. Murray, Michael S. McCormick, Boi Hanh Huynh
Publikováno v:
Biochemistry. 46:14795-14809
At its carboxylate-bridged diiron active site, the hydroxylase component of toluene/o-xylene monooxygenase activates dioxygen for subsequent arene hydroxylation. In an I100W variant of this enzyme, we characterized the formation and decay of two spec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dbcd61ffbf685f813ac9be30f2b5f48d
https://doi.org/10.1021/bi7017128
https://doi.org/10.1021/bi7017128