Zobrazeno 1 - 10
of 31
pro vyhledávání: '"C.A. Gormal"'
Autor:
Shirley A. Fairhurst, Kylie A. Vincent, Stephen P. Best, Christopher J. Pickett, Barry E. Smith, C.A. Gormal, Saad Khalil Ibrahim
Publikováno v:
Chemistry - A European Journal. 10:4770-4776
The first electrochemical and infra-red data on the binding of cyanide to the isolated iron-molybdenum cofactor of nitrogenase, FeMoco, is described. It is shown that cyanide stabilises a hitherto unrecognised, low-spin, EPR-active (S= 1/2), superoxi
Autor:
Stephen P. Best, Kylie A. Vincent, Christopher J. Pickett, C.A. Gormal, Barry E. Smith, Saad Khalil Ibrahim
Publikováno v:
Chemistry - A European Journal. 9:76-87
The electron-transfer chemistry of the isolated iron-molybdenum cofactor of nitrogenase (FeMoco) has been studied by electrochemical and spectroelectrochemical methods. Two interconverting forms of the cofactor arise froma redox-linked ligand isomeri
Publikováno v:
Journal of Molecular Biology. 292:871-891
The X-ray crystal structure of Klebsiella pneumoniae nitrogenase component 1 (Kp1) has been determined and refined to a resolution of 1.6 A, the highest resolution reported for any nitrogenase structure. Models derived from three 1.6 A resolution X-r
Autor:
T. Le Gall, Shirley A. Fairhurst, C.A. Gormal, Saad Khalil Ibrahim, Marcus C. Durrant, Richard A. Henderson, Christopher J. Pickett, Barry E. Smith, K.L.C. Grönberg
Publikováno v:
Coordination Chemistry Reviews. :669-687
There is strong evidence that the iron-molybdenum cofactor (FeMoco) of nitrogenase forms part of the enzyme’s active site. FeMoco, a MoFe7S9·homocitrate cluster, can be extracted intact from the enzyme into N-methylformamide solution but is report
Autor:
Ralf Schneider, Richard W. Strange, S. Samar Hasnain, C.A. Gormal, C. David Garner, Raymond L. Richards, Ian Harvey, Barry E. Smith
Publikováno v:
Inorganica Chimica Acta. :150-158
The binding of ligands to the iron-molybdenum cofactor (FeMoco) from Klebsiella pneumoniae nitrogenase has been studied by XANES and EXAFS at the Fe. Mo and Se k-edges and by EPR. Ligands investigated include the anions derived from thiophenol, 2-bro
Publikováno v:
Biochemical Journal. 322:737-744
MgADP - reacted with the nitrogenase molybdenum–iron (MoFe) protein of Klebsiella pneumoniae (Kp1) over a period of 2 h to yield a stable, catalytically active conjugate. The isolated protein exhibited a new, broad 31 P NMR resonance at -1 p.p.m. l
Publikováno v:
The Journal of biological chemistry. 277(38)
The x-ray crystal structure of NifV− Klebsiella pneumoniae nitrogenase MoFe protein (NifV− Kp1) has been determined and refined to a resolution of 1.9 A. This is the first structure for a nitrogenase MoFe protein with an altered cofactor. Moreove
Publikováno v:
Nitrogen Fixation: From Molecules to Crop Productivity ISBN: 9780792362333
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cb7f715224163002aa2ceddeb8239c84
https://doi.org/10.1007/0-306-47615-0_7
https://doi.org/10.1007/0-306-47615-0_7
Autor:
Kylie A. Vincent, Christopher J. Pickett, Saad K. Ibrahim, Steven P. Best, Barry E. Smith, C.A. Gormal
Publikováno v:
Scopus-Elsevier
The first spectroscopic evidence for the binding of a small gaseous molecule to the isolated iron molybdenum cofactor of nitrogenase (FeMoco) is presented: FTIR spectroelectrochemistry in a thin-layer cell shows that reduced FeMoco binds carbon monox
Autor:
S. Samar Hasnain, S.M. Roe, Robert R. Eady, David M. Lawson, Faridoon K. Yousafzai, C.A. Gormal, S.M. Mayer, J.G. Grossmann, Barry E. Smith
Publikováno v:
Biological Nitrogen Fixation for the 21st Century ISBN: 9789401061698
The 3D crystallographic structure of the nitrogenase MoFe protein was first determined for the protein from Azotobacter vinelandii (Av1) at 2.8 A resolution and identified two unique metal-sulphur clusters viz the FeMoco centres and the P clusters (K
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0fd8115a10a1494b079a59f63ab1f3fc
https://doi.org/10.1007/978-94-011-5159-7_9
https://doi.org/10.1007/978-94-011-5159-7_9