Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Caleb J. Hiller"'
Autor:
Joseph B. Solomon, Mahtab F. Rasekh, Caleb J. Hiller, Chi Chung Lee, Kazuki Tanifuji, Markus W. Ribbe, Yilin Hu
Publikováno v:
JACS Au, Vol 1, Iss 2, Pp 119-123 (2020)
Externí odkaz:
https://doaj.org/article/54f4a632e5d24cbf8216940040db48da
Autor:
Lee A. Rettberg, Wonchull Kang, Martin T. Stiebritz, Caleb J. Hiller, Chi Chung Lee, Jasper Liedtke, Markus W. Ribbe, Yilin Hu
Publikováno v:
mBio, Vol 10, Iss 4 (2019)
ABSTRACT Nitrogenase iron (Fe) proteins reduce CO2 to CO and/or hydrocarbons under ambient conditions. Here, we report a 2.4-Å crystal structure of the Fe protein from Methanosarcina acetivorans (MaNifH), which is generated in the presence of a redu
Externí odkaz:
https://doaj.org/article/b8db188bd46a4cd2bf01b2ab9361b821
Autor:
Yilin Hu, Nathaniel S. Sickerman, Kazuki Tanifuji, Yasuhiro Ohki, Chi Chung Lee, Martin T. Stiebritz, Caleb J. Hiller
Publikováno v:
Nature Catalysis. 1:444-451
The Fe protein of nitrogenase contains a redox active [Fe4S4] cluster that plays a key role in electron transfer and substrate reduction. Here we show that the Fe protein of Methanosarcina acetivorans can reduce CO2 and CO to hydrocarbons under ambie
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1aa2c7659379e1ea9a0b708cfe472bad
https://doi.org/10.1038/s41929-018-0079-4
https://doi.org/10.1038/s41929-018-0079-4
Autor:
Jasper Liedtke, Chi Chung Lee, Markus W. Ribbe, Caleb J. Hiller, Wonchull Kang, Martin T. Stiebritz, Yilin Hu, Lee A. Rettberg
Publikováno v:
mBio, Vol 10, Iss 4 (2019)
mBio, Vol 10, Iss 4, p e01497-19 (2019)
mBio
mBio, Vol 10, Iss 4, p e01497-19 (2019)
mBio
This work reports the crystal structure of a previously uncharacterized Fe protein from a methanogenic organism, which provides important insights into the structural properties of the less-characterized, yet highly interesting archaeal nitrogenase e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e9013f02070f27a68fdf8a9e287209e0
https://doi.org/10.1128/mbio.01497-19
https://doi.org/10.1128/mbio.01497-19
Publikováno v:
Chemistry (Weinheim an der Bergstrasse, Germany). 25(10)
Nitrogenase utilizes an ATP-dependent reductase to deliver electrons to its catalytic component to enable two important reactions: the reduction of N2 to NH4+ , and the reduction of CO to hydrocarbons. The two nitrogenase-based reactions parallel the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::51c84236fee48cd3b4cba724093b202a
https://pubmed.ncbi.nlm.nih.gov/30225894
https://pubmed.ncbi.nlm.nih.gov/30225894
Publikováno v:
Angewandte Chemie (International ed. in English), vol 57, iss 13
Binding and activation of CO by nitrogenase is a topic of interest because CO is isoelectronic to N(2), the physiological substrate of this enzyme. Here we examine the catalytic relevance of one- and multi-CO-bound states (i.e., the lo- and hi-CO sta
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::78c784d86cf77c2bbfdd9c24fa249a11
https://escholarship.org/uc/item/0140b45z
https://escholarship.org/uc/item/0140b45z
Publikováno v:
Structure and Bonding ISBN: 9783030258962
Nitrogenase catalyzes the remarkable chemical transformations of N2 to NH3, and C1 substrates to hydrocarbons, under ambient conditions. The best-studied Mo-nitrogenase utilizes a complex metallocofactor ([MoFe7S9C(R-homocitrate)]) for substrate bind
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d1a8db654ae437e37a386849301585a3
https://doi.org/10.1007/430_2018_29
https://doi.org/10.1007/430_2018_29
Publikováno v:
Chemistry – A European Journal. 23
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b25f9d54414e6965bbbe8362c1d16627
https://doi.org/10.1002/chem.201786463
https://doi.org/10.1002/chem.201786463