B. K. Burgess

Site-directed mutagenesis of Azotobacter vinelandii ferredoxin I: cysteine ligation of the [4Fe-4S] cluster with protein rearrangement is preferred over serine ligation.

Shen, B, Jollie, D R, Diller, T C, Stout, C D, Stephens, P J, Burgess, B K

The [4Fe-4S] cluster of Azotobacter vinelandii ferredoxin I receives three of its four ligands from a Cys-Xaa-Xaa-Cys-Xaa-Xaa-Cys sequence at positions 39-45 while the fourth ligand, Cys20, is...

Selenol binds to iron in nitrogenase iron-molybdenum cofactor: an extended x-ray absorption fine structure study.

Conradson, S D, Burgess, B K, Newton, W E, Di Cicco, A, Filipponi, A, Wu, Z Y, ...

The biological N2-fixation reaction is catalyzed by the enzyme nitrogenase. The metal cluster active site of this enzyme, the iron-molybdenum cofactor (FeMoco), can be studied either while bound...

Site-directed mutagenesis of Azotobacter vinelandii ferredoxin I: [Fe-S] cluster-driven protein rearrangement.

Martín, A E, Burgess, B K, Stout, C D, Cash, V L, Dean, D R, Jensen, G M, ...

Azotobacter vinelandii ferredoxin I is a small protein that contains one [4Fe-4S] cluster and one [3Fe-4S] cluster. Recently the x-ray crystal structure has been redetermined and the fdxA gene, which...

Azotobacter vinelandii mutS: nucleotide sequence and mutant analysis.

Le, O, Shen, B, Iismaa, S E, Burgess, B K

An Azotobacter vinelandii homolog to the Salmonella typhimurium mutS gene was discovered upstream of the fdxA gene. The product of this gene is much more similar to S. typhimurium MutS than either is...

Construction and characterization of an Azotobacter vinelandii strain with mutations in the genes encoding flavodoxin and ferredoxin I.

Martin, A E, Burgess, B K, Iismaa, S E, Smartt, C T, Jacobson, M R, Dean, D R

Flavodoxin and ferredoxin I have both been implicated as components of the electron transport chain to nitrogenase in the aerobic bacterium Azotobacter vinelandii. Recently, the genes encoding...

Activity, reconstitution, and accumulation of nitrogenase components in Azotobacter vinelandii mutant strains containing defined deletions within the nitrogenase structural gene cluster.

Robinson, A C, Burgess, B K, Dean, D R

The Azotobacter vinelandii genes encoding the nitrogenase structural components are clustered and ordered: nifH (Fe protein)-nifD (MoFe protein alpha subunit)-nifK (MoFe protein beta subunit). In...

Spectroscopic studies of ferricyanide oxidation of Azotobacter vinelandii ferredoxin I.

Morgan, T V, Stephens, P J, Devlin, F, Stout, C D, Melis, K A, Burgess, B K

The Fe(CN)3-(6) oxidation of the crystallographically characterized [[3Fe-3S], [4Fe-4S]] ferredoxin I of Azotobacter vinelandii has been studied using absorption, circular dichroism, magnetic...

Fluorine-19 chemical shifts as structural probes of metal-sulfur clusters and the cofactor of nitrogenase.

Mascharak, P K, Smith, M C, Armstrong, W H, Burgess, B K, Holm, R H

Several properties of the FeMo-cofactor (co) of nitrogenase in N-methylformamide solution at ambient temperature have been investigated by means of 19F NMR spectroscopy. With C6H5CF3 reference...

[4Fe-4S]-cluster-depleted Azotobacter vinelandii ferredoxin I: a new 3Fe iron-sulfur protein.

Stephens, P J, Morgan, T V, Devlin, F, Penner-Hahn, J E, Hodgson, K O, Scott, R A, ...

Fe(CN)6(-3) oxidation of the aerobically isolated 7Fe Azotobacter vinelandii ferredoxin I, (7Fe)FdI, is a degradative reaction. Destruction of the [4Fe-4S] cluster occurs first, followed by...

Identification of iron-sulfur centers in the iron-molybdenum proteins of nitrogenase.

Kurtz, D M, McMillan, R S, Burgess, B K, Mortenson, L E, Holm, R H

The core extrusion method has been applied to the determination of the type ([2Fe-2S], [4Fe-4S]) and number of iron-sulfur centers in the FeMo proteins of the nitrogenases from Clostridium...

Analysis of Azotobacter vinelandii strains containing defined deletions in the nifD and nifK genes.

Li, J G, Tal, S, Robinson, A C, Dang, V, Burgess, B K

Strains of Azotobacter vinelandii which contain defined deletions within the nifD and nifK genes which encode, respectively, the alpha and beta subunits of the MoFe protein of nitrogenase were...

Influence of electrochemical properties in determining the sensitivity of [4Fe-4S] clusters in proteins to oxidative damage.

Tilley, G J, Camba, R, Burgess, B K, Armstrong, F A

Interconversion between [4Fe-4S] cubane and [3Fe-4S] cuboidal states represents one of the simplest structural changes an iron-sulphur cluster can undertake. This reaction is implicated in oxidative...

Site-directed mutagenesis of Azotobacter vinelandii ferredoxin I: cysteine ligation of the [4Fe-4S] cluster with protein rearrangement is preferred over serine ligation.

Shen, B, Jollie, D R, Diller, T C, Stout, C D, Stephens, P J, Burgess, B K

The [4Fe-4S] cluster of Azotobacter vinelandii ferredoxin I receives three of its four ligands from a Cys-Xaa-Xaa-Cys-Xaa-Xaa-Cys sequence at positions 39-45 while the fourth ligand, Cys20, is...

Selenol binds to iron in nitrogenase iron-molybdenum cofactor: an extended x-ray absorption fine structure study.

Conradson, S D, Burgess, B K, Newton, W E, Di Cicco, A, Filipponi, A, Wu, Z Y, ...

The biological N2-fixation reaction is catalyzed by the enzyme nitrogenase. The metal cluster active site of this enzyme, the iron-molybdenum cofactor (FeMoco), can be studied either while bound...

Site-directed mutagenesis of Azotobacter vinelandii ferredoxin I: [Fe-S] cluster-driven protein rearrangement.

Martín, A E, Burgess, B K, Stout, C D, Cash, V L, Dean, D R, Jensen, G M, ...

Azotobacter vinelandii ferredoxin I is a small protein that contains one [4Fe-4S] cluster and one [3Fe-4S] cluster. Recently the x-ray crystal structure has been redetermined and the fdxA gene, which...

Azotobacter vinelandii mutS: nucleotide sequence and mutant analysis.

Le, O, Shen, B, Iismaa, S E, Burgess, B K

An Azotobacter vinelandii homolog to the Salmonella typhimurium mutS gene was discovered upstream of the fdxA gene. The product of this gene is much more similar to S. typhimurium MutS than either is...

Construction and characterization of an Azotobacter vinelandii strain with mutations in the genes encoding flavodoxin and ferredoxin I.

Martin, A E, Burgess, B K, Iismaa, S E, Smartt, C T, Jacobson, M R, Dean, D R

Flavodoxin and ferredoxin I have both been implicated as components of the electron transport chain to nitrogenase in the aerobic bacterium Azotobacter vinelandii. Recently, the genes encoding...

Activity, reconstitution, and accumulation of nitrogenase components in Azotobacter vinelandii mutant strains containing defined deletions within the nitrogenase structural gene cluster.

Robinson, A C, Burgess, B K, Dean, D R

The Azotobacter vinelandii genes encoding the nitrogenase structural components are clustered and ordered: nifH (Fe protein)-nifD (MoFe protein alpha subunit)-nifK (MoFe protein beta subunit). In...

Spectroscopic studies of ferricyanide oxidation of Azotobacter vinelandii ferredoxin I.

Morgan, T V, Stephens, P J, Devlin, F, Stout, C D, Melis, K A, Burgess, B K

The Fe(CN)3-(6) oxidation of the crystallographically characterized [[3Fe-3S], [4Fe-4S]] ferredoxin I of Azotobacter vinelandii has been studied using absorption, circular dichroism, magnetic...

Fluorine-19 chemical shifts as structural probes of metal-sulfur clusters and the cofactor of nitrogenase.

Mascharak, P K, Smith, M C, Armstrong, W H, Burgess, B K, Holm, R H

Several properties of the FeMo-cofactor (co) of nitrogenase in N-methylformamide solution at ambient temperature have been investigated by means of 19F NMR spectroscopy. With C6H5CF3 reference...

[4Fe-4S]-cluster-depleted Azotobacter vinelandii ferredoxin I: a new 3Fe iron-sulfur protein.

Stephens, P J, Morgan, T V, Devlin, F, Penner-Hahn, J E, Hodgson, K O, Scott, R A, ...

Fe(CN)6(-3) oxidation of the aerobically isolated 7Fe Azotobacter vinelandii ferredoxin I, (7Fe)FdI, is a degradative reaction. Destruction of the [4Fe-4S] cluster occurs first, followed by...

Identification of iron-sulfur centers in the iron-molybdenum proteins of nitrogenase.

Kurtz, D M, McMillan, R S, Burgess, B K, Mortenson, L E, Holm, R H

The core extrusion method has been applied to the determination of the type ([2Fe-2S], [4Fe-4S]) and number of iron-sulfur centers in the FeMo proteins of the nitrogenases from Clostridium...

Analysis of Azotobacter vinelandii strains containing defined deletions in the nifD and nifK genes.

Li, J G, Tal, S, Robinson, A C, Dang, V, Burgess, B K

Strains of Azotobacter vinelandii which contain defined deletions within the nifD and nifK genes which encode, respectively, the alpha and beta subunits of the MoFe protein of nitrogenase were...

Influence of electrochemical properties in determining the sensitivity of [4Fe-4S] clusters in proteins to oxidative damage.

Tilley, G J, Camba, R, Burgess, B K, Armstrong, F A

Interconversion between [4Fe-4S] cubane and [3Fe-4S] cuboidal states represents one of the simplest structural changes an iron-sulphur cluster can undertake. This reaction is implicated in oxidative...

The crystal structure of NADPH:ferredoxin reductase from Azotobacter vinelandii.

Sridhar Prasad, G., Kresge, N., Muhlberg, A. B., Shaw, A., Jung, Y. S., Burgess, B. K., ...

NADPH:ferredoxin reductase (AvFPR) is involved in the response to oxidative stress in Azotobacter vinelandii. The crystal structure of AvFPR has been determined at 2.0 A resolution. The polypeptide...