Zobrazeno 1 - 10
of 10
pro vyhledávání: '"L. C. Seefeldt"'
Autor:
K. H. Tibelius, R. P. Garg, Daniel J. Arp, L. C. Seefeldt, Nisha Garg, C. M. Ford, M. G. Yates
Publikováno v:
Molecular Microbiology. 4:999-1008
The structural genes (hupSL) of the membrane-bound NiFe-containing H2-uptake hydrogenase (Hup) of Azotobacter chroococcum were identified by oligonucleotide screening and sequenced. The small subunit gene (hupS) encodes a signal sequence of 34 amino
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a2f8f664f2128ef5c7ac69a1f58c26b8
https://doi.org/10.1111/j.1365-2958.1990.tb00672.x
https://doi.org/10.1111/j.1365-2958.1990.tb00672.x
Autor:
R. Y. Igarashi, L. C. Seefeldt
Publikováno v:
Catalysts for Nitrogen Fixation ISBN: 9789048166756
The biological fixation of N2 occurs in select prokaryotes, with representatives in both the bacteria and the archaea (Madigan et al., 2003). In all cases, the initial reduction of N2 to ammonia is catalyzed by the enzyme nitrogenase. There are two d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::67a7090be8f16b3da73131ceae3e0f89
https://doi.org/10.1007/978-1-4020-3611-8_5
https://doi.org/10.1007/978-1-4020-3611-8_5
Autor:
W. N. Lanzilotta, L. C. Seefeldt
Publikováno v:
Biological Nitrogen Fixation for the 21st Century ISBN: 9789401061698
Nitrogenase catalyzed substrate reduction requires electron transfer between two component proteins, the iron (Fe) protein and the molybdenum-iron (MoFe) protein in a reaction coupled to MgATP hydrolysis. Previous studies suggest that a single electr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::37406dbb2163edef4cb7a58b3fa4efa3
https://doi.org/10.1007/978-94-011-5159-7_22
https://doi.org/10.1007/978-94-011-5159-7_22
Publikováno v:
Biological Nitrogen Fixation for the 21st Century ISBN: 9789401061698
The MoFe protein from Azotobacter vinelandii (AvI) and the Fe protein from Clostridium pasteurianum (CpII) form a tight complex with an association constant about 10-fold higher than that for the homologous A. vinelandii Fe protein (AvII) - AvI compl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::42b7da4d77264b9468c69f85bc09eb72
https://doi.org/10.1007/978-94-011-5159-7_21
https://doi.org/10.1007/978-94-011-5159-7_21
Publikováno v:
The Journal of biological chemistry. 272(7)
Nitrogenase-catalyzed substrate reduction reactions require the association of the iron (Fe) protein and the molybdenum-iron (MoFe) protein, electron transfer from the Fe protein to the MoFe protein coupled to the hydrolysis of MgATP, followed by pro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::651e1dd420da040f9be9ac031ed8c62d
https://pubmed.ncbi.nlm.nih.gov/9020128
https://pubmed.ncbi.nlm.nih.gov/9020128
Publikováno v:
The Journal of biological chemistry. 271(3)
Nucleotide interactions with nitrogenase are a central part of the mechanism of nitrogen reduction. Previous studies have suggested that MgATP or MgADP binding to the nitrogenase iron protein (Fe protein) induce protein conformational changes that co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::58582ebe55b047b681a336609269a64f
https://pubmed.ncbi.nlm.nih.gov/8576152
https://pubmed.ncbi.nlm.nih.gov/8576152
Publikováno v:
Advances in enzymology and related areas of molecular biology. 67
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::725681b7a2c07ffd06c7df7f3d9642fb
https://pubmed.ncbi.nlm.nih.gov/8322617
https://pubmed.ncbi.nlm.nih.gov/8322617
Publikováno v:
The Journal of biological chemistry. 267(10)
Nitrogenase binds and hydrolyzes 2MgATP yielding 2MgADP and 2Pi for each electron that is transferred from the iron protein to the MoFe protein. The iron protein alone binds but does not hydrolyze 2MgATP or 2MgADP and the binding of these nucleotides
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::0738e81ec209f380491f6d7463b38383
https://pubmed.ncbi.nlm.nih.gov/1313018
https://pubmed.ncbi.nlm.nih.gov/1313018
Publikováno v:
The Journal of biological chemistry. 261(23)
Hydrogenases catalyze the reversible activation of dihydrogen. The hydrogenases from the aerobic, N2-fixing microorganisms Azotobacter vinelandii and Rhizobium japonicum are nickel- and iron-containing dimers that belong to the group of O2-labile enz
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b524ef2e9c6eb542b770f22cbead2eba
https://pubmed.ncbi.nlm.nih.gov/3525552
https://pubmed.ncbi.nlm.nih.gov/3525552
Autor:
L C, Seefeldt, D J, Arp
Publikováno v:
The Journal of biological chemistry. 262(35)
Hydrogenases catalyze the reversible activation of dihydrogen. We have previously demonstrated that the purified hydrogenase from the nitrogen-fixing microorganism Azotobacter vinelandii is an alpha beta dimer (98,000 Da) with subunits of 67,000 (alp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::7149c819565db439cd29cd64703c7198
https://pubmed.ncbi.nlm.nih.gov/3316226
https://pubmed.ncbi.nlm.nih.gov/3316226