Zobrazeno 1 - 10
of 30
pro vyhledávání: '"Thomas, Spatzal"'
Autor:
Lorenz Heidinger, Kathryn Perez, Thomas Spatzal, Oliver Einsle, Stefan Weber, Douglas C. Rees, Erik Schleicher
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-15 (2024)
Abstract Due to the complexity of the catalytic FeMo cofactor site in nitrogenases that mediates the reduction of molecular nitrogen to ammonium, mechanistic details of this reaction remain under debate. In this study, selenium- and sulfur-incorporat
Externí odkaz:
https://doaj.org/article/3533319ff4c04865b13a91688453b6fa
Autor:
Thomas Spatzal, Julia Schlesier, Eva-Maria Burger, Daniel Sippel, Limei Zhang, Susana L.A. Andrade, Douglas C. Rees, Oliver Einsle
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-7 (2016)
The [Mo:7Fe:9S:C] iron-molybdenum cofactor (FeMoco) of nitrogenase is a large metal cluster with an important role in biological nitrogen fixation. Here, the authors use spatially resolved refinement of the anomalous scattering contributions of the i
Externí odkaz:
https://doaj.org/article/7d51f7faadfe4a1385e5a5ac269c9d7a
Autor:
Martin L. Kirk, Thomas W. Hercher, Corinna Probst, Jing Yang, Tobias Kruse, Khadanand Kc, Douglas C. Rees, Thomas Spatzal, Joern Krausze, Logan J. Giles, Ralf R. Mendel, Casseday P. Richers
Publikováno v:
Nature chemistry
The molybdenum cofactor (Moco) is found in the active site of numerous important enzymes that are critical to biological processes. The bidentate ligand that chelates molybdenum (Mo) in Moco is the pyranopterin dithiolene (molybdopterin, MPT); howeve
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fee12bca971ba63979d4c3ca2bd4ba4c
https://doi.org/10.1038/s41557-021-00714-1
https://doi.org/10.1038/s41557-021-00714-1
Publikováno v:
Angewandte Chemie (International Ed. in English)
As an approach towards unraveling the nitrogenase mechanism, we have studied the binding of CO to the active‐site FeMo‐cofactor. CO is not only an inhibitor of nitrogenase, but it is also a substrate, undergoing reduction to hydrocarbons (Fischer
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::905cc6cec41298a0608bcf7ec72fd6c4
https://doi.org/10.1002/ange.202015751
https://doi.org/10.1002/ange.202015751
Publikováno v:
eLife, Vol 4 (2015)
Dinitrogen reduction in the biological nitrogen cycle is catalyzed by nitrogenase, a two-component metalloenzyme. Understanding of the transformation of the inert resting state of the active site FeMo-cofactor into an activated state capable of reduc
Externí odkaz:
https://doaj.org/article/0cdb2a0894bb42d2ba78050463fd7b8d
Publikováno v:
Angewandte Chemie (International Ed. in English)
The nitrogenase iron protein (Fe‐protein) contains an unusual [4Fe:4S] iron‐sulphur cluster that is stable in three oxidation states: 2+, 1+, and 0. Here, we use spatially resolved anomalous dispersion (SpReAD) refinement to determine oxidation a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a2dbc779720765533e1f8e6597e6e5dc
http://europepmc.org/articles/PMC6519357
http://europepmc.org/articles/PMC6519357
Publikováno v:
Protein Science : A Publication of the Protein Society
Azotobacter vinelandii flavodoxin II serves as a physiological reductant of nitrogenase, the enzyme system mediating biological nitrogen fixation. Wildtype A. vinelandii flavodoxin II was electrochemically and crystallographically characterized to be
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d87ced79dd7622e90bf46d85144482b0
http://europepmc.org/articles/PMC5606536
http://europepmc.org/articles/PMC5606536
Publikováno v:
Journal of the American Chemical Society
Protonated states of the nitrogenase active site are mechanistically significant since substrate reduction is invariably accompanied by proton uptake. We report the low pH characterization by X-ray crystallography and EPR spectroscopy of the nitrogen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f1704ba719c4988cbf4a564fcbb9e288
https://doi.org/10.1021/jacs.7b05695
https://doi.org/10.1021/jacs.7b05695
Production and isolation of vanadium nitrogenase from Azotobacter vinelandii by molybdenum depletion
Autor:
Susana L. A. Andrade, Michael Rohde, Ivana Djurdjevic, Daniel Sippel, Julia Schlesier, Christian Trncik, Thomas Spatzal, Oliver Einsle, Laure Decamps
Publikováno v:
JBIC Journal of Biological Inorganic Chemistry. 22:161-168
The alternative, vanadium-dependent nitrogenase is employed by Azotobacter vinelandii for the fixation of atmospheric N2 under conditions of molybdenum starvation. While overall similar in architecture and functionality to the common Mo-nitrogenase,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1e56cb316e4774b548ea3652ae52b636
https://doi.org/10.1007/s00775-016-1423-2
https://doi.org/10.1007/s00775-016-1423-2
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 1876
Nitrogenase is the only known enzymatic system capable of reducing atmospheric dinitrogen to ammonia. This unique reaction requires tightly choreographed interactions between the nitrogenase component proteins, the molybdenum-iron (MoFe)- and iron (F
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::3f841aff42b655ef68f81398b7af2035
https://pubmed.ncbi.nlm.nih.gov/30317480
https://pubmed.ncbi.nlm.nih.gov/30317480