Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Belinda B. Wenke"'
Autor:
Rebeccah A. Warmack, Ailiena O. Maggiolo, Andres Orta, Belinda B. Wenke, James B. Howard, Douglas C. Rees
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-10 (2023)
Abstract Nitrogenase catalyzes the ATP-dependent reduction of dinitrogen to ammonia during the process of biological nitrogen fixation that is essential for sustaining life. The active site FeMo-cofactor contains a [7Fe:1Mo:9S:1C] metallocluster coor
Externí odkaz:
https://doaj.org/article/be832672eab34ef78cf20fb18ca4bfdc
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:
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
Publikováno v:
Methods in Molecular Biology ISBN: 9781493988631
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=doi_________::b743a92e9a1eab3879ddbd6217cdc6c4
https://doi.org/10.1007/978-1-4939-8864-8_10
https://doi.org/10.1007/978-1-4939-8864-8_10
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 82:528-534
The X-ray structures of the hemoglobin from Synechococcus sp. PCC 7002 (GlbN) were solved in the ferric bis-histidine (1.44 A resolution) and cyanide-bound (2.25 A resolution) states with covalently attached heme. The two structures illustrate the co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0facb5f2041bd8a7b6f72fe62cfc403d
https://doi.org/10.1002/prot.24409
https://doi.org/10.1002/prot.24409
Autor:
Juliette T. J. Lecomte, Belinda B. Wenke, Matthew P. Pond, Matthew R. Preimesberger, Lukas Gilevicius
Publikováno v:
Biochemistry. 52:3478-3488
Iron-protoporphyrin IX, or b heme, is utilized as such by a large number of proteins and enzymes. In some cases, notably the c-type cytochromes, this group undergoes a posttranslational covalent attachment to the polypeptide chain, which adjusts the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0c22c154642e441372450349b4b74156
https://doi.org/10.1021/bi400289e
https://doi.org/10.1021/bi400289e
Autor:
Lukas Gilevicius, Jason M. Brown, Dillon B. Nye, Matthew R. Preimesberger, Belinda B. Wenke, Eric A. Johnson, George B. Witman, Juliette T. J. Lecomte, Selena L. Rice
Publikováno v:
Biochemistry
The nuclear genome of the model organism Chlamydomonas reinhardtii contains genes for a dozen hemoglobins of the truncated lineage. Of those, THB1 is known to be expressed, but the product and its function have not yet been characterized. We present
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2c48b94baca6873c7b1927c2139b5af7
https://pubmed.ncbi.nlm.nih.gov/24964018
https://pubmed.ncbi.nlm.nih.gov/24964018
The cis-syn thymine cyclobutane dimer is a DNA photoproduct implicated in skin cancer. We compared the stability of individual base pairs in thymine dimer-containing duplexes to undamaged parent 10-mer duplexes. UV melting thermodynamic measurements,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::910cd7f050deb78ea7815d5d476bdaa2
https://europepmc.org/articles/PMC3912563/
https://europepmc.org/articles/PMC3912563/
Publikováno v:
Proteins. 82(3)
The X-ray structures of the hemoglobin from Synechococcus sp. PCC 7002 (GlbN) were solved in the ferric bis-histidine (1.44 Å resolution) and cyanide-bound (2.25 Å resolution) states with covalently attached heme. The two structures illustrate the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::384f332419147e278f151eb67d6627db
https://pubmed.ncbi.nlm.nih.gov/23999883
https://pubmed.ncbi.nlm.nih.gov/23999883
Autor:
Juliette T. J. Lecomte, Selena L. Rice, Matthew P. Pond, Matthew R. Preimesberger, Belinda B. Wenke
Publikováno v:
Chemistrybiodiversity. 9(9)
The hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002 (GlbN) contains three tyrosines (Tyr5, Tyr22, and Tyr53), each of which undergoes a structural rearrangement when the protein binds an exogenous ligand such as cyanide. We explored the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1f646ef916e8372b916484e2c8ea5186
https://pubmed.ncbi.nlm.nih.gov/22976963
https://pubmed.ncbi.nlm.nih.gov/22976963