Zobrazeno 1 - 10
of 164
pro vyhledávání: '"M, Sahlin"'
Publikováno v:
Midwifery. 29:447-452
Background: international estimates suggest that caesarean section on maternal request range from 4% to 18% of all caesarean section. An increasing number of surveys have investigated women’s reasons for a caesarean section in the absence of a medi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8dbc72fd3d7a5d5cd9b513ca839c323c
https://doi.org/10.1016/j.midw.2012.02.009
https://doi.org/10.1016/j.midw.2012.02.009
Publikováno v:
Journal of Biological Chemistry. 269:5595-5601
The formation of the iron-radical cofactor in the R2 subunit of ribonucleotide reductase has been monitored by resonance Raman spectroscopy. The differrous cluster in reduced R2 functions as a tyrosine oxidase; it uses O2 to oxidize Tyr-122 to a stab
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d84f8ac562262938cab3b23176028ccb
https://doi.org/10.1016/s0021-9258(17)37503-8
https://doi.org/10.1016/s0021-9258(17)37503-8
Akademický článek
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Autor:
M, Sahlin, B M, Sjöberg
Publikováno v:
Sub-cellular biochemistry. 35
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::ae98ff7324e9ce2bb88c378c14882f27
https://pubmed.ncbi.nlm.nih.gov/11192729
https://pubmed.ncbi.nlm.nih.gov/11192729
Akademický článek
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Publikováno v:
The Journal of biological chemistry. 275(26)
Class III ribonucleotide reductase (RNR) is an anaerobic glycyl radical enzyme that catalyzes the reduction of ribonucleotides to deoxyribonucleotides. We have investigated the importance in the reaction mechanism of nine conserved cysteine residues
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::dd4317785e2fd6447b10bee0f556f736
https://pubmed.ncbi.nlm.nih.gov/10748010
https://pubmed.ncbi.nlm.nih.gov/10748010
Publikováno v:
Advances in experimental medicine and biology. 469
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::e5922e3902bc66c60d18a4ed7b2f3e8d
https://pubmed.ncbi.nlm.nih.gov/10667399
https://pubmed.ncbi.nlm.nih.gov/10667399
Publikováno v:
The Journal of biological chemistry. 273(33)
A hydrogen-bonded catalytic radical transfer pathway in Escherichia coli ribonucleotide reductase (RNR) is evident from the three-dimensional structures of the R1 and R2 proteins, phylogenetic studies, and site-directed mutagenesis experiments. Curre
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b97d0563318e713ad6a59c5888e87f66
https://pubmed.ncbi.nlm.nih.gov/9694851
https://pubmed.ncbi.nlm.nih.gov/9694851
Publikováno v:
The Journal of biological chemistry. 272(16)
Reconstitution of the tyrosyl radical in ribonucleotide reductase protein R2 requires oxidation of a diferrous site by oxygen. The reaction involves one externally supplied electron in addition to the three electrons provided by oxidation of the Tyr-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::26af9b74e1283bbacc45c2cd3ae0beae
https://pubmed.ncbi.nlm.nih.gov/9099682
https://pubmed.ncbi.nlm.nih.gov/9099682
Publikováno v:
The Journal of biological chemistry. 270(21)
Ferrous iron/oxygen reconstitution of the mutant R2 apoprotein Y122F leads to formation of a diferric center similar to that of the wild-type R2 protein of Escherichia coli ribonucleotide reductase. This reconstitution reaction requires two extra ele
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::8c3d381d325a5c9e8ac2e85915e4de07
https://pubmed.ncbi.nlm.nih.gov/7759477
https://pubmed.ncbi.nlm.nih.gov/7759477