Redox reactions of and nucleotide binding to the iron protein of Azotobacter vinelandii

G. D. Watt; Z. C. Wang; R. R. Knotts

doi:10.1021/bi00373a005

Redox reactions of and nucleotide binding to the iron protein of Azotobacter vinelandii

Biochemistry ◽

10.1021/bi00373a005 ◽

1986 ◽

Vol 25 (25) ◽

pp. 8156-8162 ◽

Cited By ~ 45

Author(s):

G. D. Watt ◽

Z. C. Wang ◽

R. R. Knotts

Keyword(s):

Redox Reactions ◽

Azotobacter Vinelandii ◽

Nucleotide Binding ◽

Iron Protein

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Further redox reactions of metal clusters in the molybdenum-iron protein of Azotobacter vinelandii nitrogenase

Biochemistry ◽

10.1021/bi00366a032 ◽

1986 ◽

Vol 25 (18) ◽

pp. 5196-5202 ◽

Cited By ~ 8

Author(s):

G. D. Watt ◽

Z. Wang

Keyword(s):

Redox Reactions ◽

Metal Clusters ◽

Azotobacter Vinelandii ◽

Molybdenum Iron Protein ◽

Iron Protein

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Mapping the site(s) of MgATP and MgADP interaction with the nitrogenase of Azotobacter vinelandii. Lysine 15 of the iron protein plays a major role in MgATP interaction.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)50480-x ◽

1992 ◽

Vol 267 (10) ◽

pp. 6680-6688

Author(s):

L.C. Seefeldt ◽

T.V. Morgan ◽

D.R. Dean ◽

L.E. Mortenson

Keyword(s):

Azotobacter Vinelandii ◽

Iron Protein

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Crystal structure of the nitrogenase iron protein from Azotobacter vinelandii

Nitrogen Fixation ◽

10.1007/978-1-4684-6432-0_12 ◽

1990 ◽

pp. 111-116 ◽

Cited By ~ 6

Author(s):

Millie M. Georgiadis ◽

Pinak Chakrabarti ◽

Douglas C. Rees

Keyword(s):

Crystal Structure ◽

Azotobacter Vinelandii ◽

Iron Protein ◽

Nitrogenase Iron Protein

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Thermodynamics of nucleotide interactions with the Azotobacter vinelandii nitrogenase iron protein

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology ◽

10.1016/s0167-4838(98)00251-9 ◽

1999 ◽

Vol 1429 (2) ◽

pp. 411-421 ◽

Cited By ~ 14

Author(s):

William N Lanzilotta ◽

Vernon D Parker ◽

Lance C Seefeldt

Keyword(s):

Azotobacter Vinelandii ◽

Iron Protein ◽

Nucleotide Interactions ◽

Nitrogenase Iron Protein

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Circular dichroism and magnetic circular dichroism of reduced molybdenum-iron protein of Azotobacter vinelandii nitrogenase

Biochemistry ◽

10.1021/bi00513a023 ◽

1981 ◽

Vol 20 (10) ◽

pp. 2857-2864 ◽

Cited By ~ 18

Author(s):

P. J. Stephens ◽

C. E. McKenna ◽

M. C. McKenna ◽

H. T. Nguyen ◽

F. Devlin

Keyword(s):

Circular Dichroism ◽

Azotobacter Vinelandii ◽

Magnetic Circular Dichroism ◽

Molybdenum Iron Protein ◽

Iron Protein ◽

Circular Dichroïsm

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Proton NMR investigation of the [4Fe-4S]1+ cluster environment of nitrogenase iron protein from Azotobacter vinelandii: defining nucleotide-induced conformational changes

Biochemistry ◽

10.1021/bi00048a007 ◽

1995 ◽

Vol 34 (48) ◽

pp. 15646-15653 ◽

Cited By ~ 17

Author(s):

William N. Lanzilotta ◽

Richard C. Holz ◽

Lance C. Seefeldt

Keyword(s):

Conformational Changes ◽

Azotobacter Vinelandii ◽

Proton Nmr ◽

Iron Protein ◽

Cluster Environment ◽

Nitrogenase Iron Protein

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Double integration and titration of the electron paramagnetic resonance signal in the molybdenum-iron protein of Azotobacter vinelandii

Biochemistry ◽

10.1021/bi00308a027 ◽

1984 ◽

Vol 23 (13) ◽

pp. 3021-3024 ◽

Cited By ~ 7

Author(s):

W. B. Euler ◽

J. Martinsen ◽

J. W. McDonald ◽

G. D. Watt ◽

Z. C. Wang

Keyword(s):

Electron Paramagnetic Resonance ◽

Electron Paramagnetic Resonance Signal ◽

Azotobacter Vinelandii ◽

Resonance Signal ◽

Paramagnetic Resonance ◽

Molybdenum Iron Protein ◽

Iron Protein ◽

Double Integration ◽

Electron Paramagnetic

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Evidence on the role(s) of atp in the mechanism of nitrogenase, from proton nmr relaxation studies on metal and nucleotide binding to the molybdenum-iron protein

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology ◽

10.1016/0167-4838(82)90261-8 ◽

1982 ◽

Vol 705 (3) ◽

pp. 385-395 ◽

Cited By ~ 5

Author(s):

Stephen J. Kimber ◽

Edward O. Bishop ◽

Barry E. Smith

Keyword(s):

Proton Nmr ◽

Nmr Relaxation ◽

Nucleotide Binding ◽

Molybdenum Iron Protein ◽

Iron Protein ◽

Relaxation Studies

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Reduction of viologen dyes and a non-haem iron protein by NADH in particles from Azotobacter vinelandii

Biochimica et Biophysica Acta (BBA) - Bioenergetics ◽

10.1016/0005-2728(67)90045-x ◽

1967 ◽

Vol 131 (1) ◽

pp. 204-207 ◽

Cited By ~ 7

Author(s):

M.S. Naik ◽

D.J.D. Nicholas

Keyword(s):

Azotobacter Vinelandii ◽

Iron Protein ◽

Haem Iron

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Isolation and partial characterization of two different subunits from the molybdenum-iron protein of Azotobacter vinelandii nitrogenase.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)34817-2 ◽

1978 ◽

Vol 253 (10) ◽

pp. 3422-3426

Author(s):

D.J. Lundell ◽

J.B. Howard

Keyword(s):

Azotobacter Vinelandii ◽

Partial Characterization ◽

Molybdenum Iron Protein ◽

Iron Protein

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