Effects on substrate reduction of substitution of histidine-195 by glutamine in the alpha-subunit of the MoFe protein of Azotobacter vinelandii nitrogenase

Studies of the substrate-reducing capabilities of an altered nitrogenase MoFe protein (alpha-195(Gln) instead of alpha-195(His)) from a mutant of Azotobacter vinelandii show, contrary to an earlier report [Kim, C.-H., Newton, W. E., and Dean, D. R. (1995) Biochemistry 34, 2798-2808], that the alpha-...

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Bibliographic Details
Published in:Biochemistry (Easton) 1998-12, Vol.37 (50), p.17495-17505
Main Authors: Dilworth, M.J. (Murdoch University, Murdoch, Western Australia.), Fisher, K, Kim, C.H, Newton, W.E
Format: Article
Language:English
Subjects:
Adenosine Triphosphate - metabolism
Amino Acid Substitution - genetics
Ammonia - metabolism
Azides - metabolism
AZOTOBACTER VINELANDII
Azotobacter vinelandii - enzymology
Azotobacter vinelandii - genetics
Cyanides - metabolism
Deuterium - metabolism
Electron Transport - genetics
FIJACION DEL NITROGENO
FIXATION DE L'AZOTE
GLUTAMINA
GLUTAMINE
Glutamine - genetics
Glutamine - metabolism
HISTIDINA
HISTIDINE
Histidine - genetics
Histidine - metabolism
Hydrogen - antagonists & inhibitors
Hydrogen - metabolism
Hydrogen-Ion Concentration
Molybdoferredoxin - genetics
Molybdoferredoxin - metabolism
Molybdoferredoxin - pharmacology
Nitrogen - metabolism
Nitrogen - physiology
NITROGEN FIXATION
NITROGENASA
NITROGENASE
Nitrogenase - antagonists & inhibitors
Nitrogenase - genetics
Nitrogenase - metabolism
Oxidation-Reduction
Oxidoreductases
Substrate Specificity - genetics
Temperature
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Summary:Studies of the substrate-reducing capabilities of an altered nitrogenase MoFe protein (alpha-195(Gln) instead of alpha-195(His)) from a mutant of Azotobacter vinelandii show, contrary to an earlier report [Kim, C.-H., Newton, W. E., and Dean, D. R. (1995) Biochemistry 34, 2798-2808], that the alpha-195(Gln) MoFe protein can reduce N2 to NH3 but at a rate that is
ISSN:0006-2960
1520-4995
DOI:10.1021/bi9812017