Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Ronda M. Allen"'
Publikováno v:
BioTechniques, Vol 33, Iss 5, Pp 1158-1165 (2002)
The QuikChange® Multi Site-Directed Mutagenesis Kit is a simple and efficient method for introducing point mutations at up to five sites simultaneously in plasmid DNA templates. Here we used the QuikChange Multi kit with degenerate (one codon) prime
Externí odkaz:
https://doaj.org/article/61c45cd876a943aca3d4492e6f486861
Publikováno v:
Journal of Biological Chemistry. 274:15869-15874
The biosynthesis of the iron-molybdenum cofactor (FeMo-co) of dinitrogenase was investigated using99Mo to follow the incorporation of Mo into precursors. 99Mo label accumulates on dinitrogenase only when all known components of the FeMo-co synthesis
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eafdc48e67c1cdb46ce1b036258f0d7a
https://doi.org/10.1074/jbc.274.22.15869
https://doi.org/10.1074/jbc.274.22.15869
Publikováno v:
Journal of Biological Chemistry. 272:21604-21608
NIFH (the nifH gene product) has several functions in the nitrogenase enzyme system. In addition to reducing dinitrogenase during nitrogenase turnover, NIFH functions in the biosynthesis of the iron-molybdenum cofactor (FeMo-co), and in the processin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f839aae94d2c40ef0486a70f5fe119e3
https://doi.org/10.1074/jbc.272.34.21604
https://doi.org/10.1074/jbc.272.34.21604
Publikováno v:
Journal of Biological Chemistry. 271:6819-6826
The vnf-encoded apodinitrogenase (apodinitrogenase 2) has been purified from Azotobacter vinelandii strain CA117.30 (DeltanifKDB), and is an alpha2beta2delta2 hexamer. Apodinitrogenase 2 can be activated in vitro by the addition of the iron-vanadium
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bfb60fc994dd7162762b4a48cfc53f76
https://doi.org/10.1074/jbc.271.12.6819
https://doi.org/10.1074/jbc.271.12.6819
Autor:
Ronda M. Allen, Dennis Flint
Publikováno v:
Chemical Reviews. 96:2315-2334
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c34d06b4ac738c35a5dda6829afbe320
https://doi.org/10.1021/cr950041r
https://doi.org/10.1021/cr950041r
Publikováno v:
Critical Reviews in Biotechnology. 14:225-249
The iron-molybdenum cofactor (FeMo-co) of nitrogenase is a unique molybdenum-containing prosthetic group that has been proposed to form an integral part of the active site of dinitrogenase. In Klebsiella pneumoniae, at least six nif (nitrogen fixatio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::97a201af5910efbafc885db14b69dfd3
https://doi.org/10.3109/07388554409079834
https://doi.org/10.3109/07388554409079834
Autor:
Mary J. Homer, Vinod K. Shah, Ranjini Chatterjee, Gary P. Roberts, Paul W. Ludden, Ronda M. Allen
Publikováno v:
Journal of Biological Chemistry. 268:23670-23674
The requirements for iron-molybdenum cofactor (FeMo-co) activation of apodinitrogenase from Azotobacter vinelandii strain UW97, which lacks dinitrogenase reductase activity as assayed by substrate reduction, have been examined. Activation of apodinit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::dbfa0fda36a910fcd4f43a0a86f34247
https://doi.org/10.1016/s0021-9258(19)49514-8
https://doi.org/10.1016/s0021-9258(19)49514-8
Autor:
Dennis Flint, Ronda M. Allen
Publikováno v:
ChemInform. 28
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8dbb2f1feaae425d54e1ca3a1ed68e90
https://doi.org/10.1002/chin.199710260
https://doi.org/10.1002/chin.199710260
Publikováno v:
Proceedings of the National Academy of Sciences. 89:6487-6491
A plausible structure of the iron-molybdenum cofactor of nitrogenase [reduced ferredoxin:dinitrogen oxidoreductase (ATP-hydrolyzing), EC 1.18.6.1] is presented based on altered substrate reduction properties of dinitrogenase containing homocitrate an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::26972e23a84353134f0d21e1e26353fc
https://doi.org/10.1073/pnas.89.14.6487
https://doi.org/10.1073/pnas.89.14.6487
Autor:
Paul W. Ludden, Ronda M. Allen, Priya Rangaraj, Gary P. Roberts, Vinod K. Shah, Jon T. Roll, Ranjini Chatterjee
The iron-molybdenum cofactor (FeMo-co) of nitrogenase contains molybdenum, iron, sulfur, and homocitrate in a ratio of 1:7:9:1. In vitro synthesis of FeMo-co has been established, and the reaction requires an ATP-regenerating system, dithionite, moly
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::03b28f03f9820e5c862a1edfb29e7114
https://europepmc.org/articles/PMC93721/
https://europepmc.org/articles/PMC93721/
