Zobrazeno 1 - 6
of 6
pro vyhledávání: '"W. N. Lanzilotta"'
Publikováno v:
Progress in nucleic acid research and molecular biology. 67
CooA, the heme-containing carbon monoxide (CO) sensor from the bacterium Rhodospirillum rubrum, is a transcriptional factor that activates expression of certain genes in response to CO. As with other heme proteins, CooA is unable to bind CO when the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::61283ffd0ec34c8d5e944d6b1e604149
https://pubmed.ncbi.nlm.nih.gov/11525385
https://pubmed.ncbi.nlm.nih.gov/11525385
Publikováno v:
Nature structural biology. 7(10)
CooA is a homodimeric transcription factor that belongs to the catabolite activator protein (CAP) family. Binding of CO to the heme groups of CooA leads to the transcription of genes involved in CO oxidation in Rhodospirillum rubrum. The 2.6 A struct
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::67ff6ed9628f067b18c605c04733c5bf
https://pubmed.ncbi.nlm.nih.gov/11017196
https://pubmed.ncbi.nlm.nih.gov/11017196
Publikováno v:
The Journal of biological chemistry. 274(28)
NifH has three different roles in the nitrogenase enzyme system. Apart from serving as the physiological electron donor to dinitrogenase, NifH is involved in iron-molybdenum cofactor (FeMo-co) biosynthesis and in maturation of the FeMo-co-deficient f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::f45b4e384f6d43b763eebe8efa183421
https://pubmed.ncbi.nlm.nih.gov/10391920
https://pubmed.ncbi.nlm.nih.gov/10391920
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:
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